Anaerobic hyperthermophilic species of ARCHAEA, isolated from hydrothermal fluid samples. It is obligately heterotrophic with coccoid cells that require TRYPTOPHAN for growth.
A genus of strictly anaerobic ultrathermophilic archaea, in the family THERMOCOCCACEAE, occurring in heated seawaters. They exhibit heterotrophic growth at an optimum temperature of 100 degrees C.
A species of strictly anaerobic, hyperthermophilic archaea which lives in geothermally-heated marine sediments. It exhibits heterotropic growth by fermentation or sulfur respiration.
Proteins found in any species of archaeon.
A species of gram-negative hyperthermophilic ARCHAEA found in deep ocean hydrothermal vents. It is an obligate anaerobe and obligate chemoorganotroph.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.
The (EXternal proTEIN) sequences flanking INTEINS, which are internal fragments of precursor proteins removed by PROTEIN SPLICING. Concomitantly, as the inteins are excised, the exteins are ligated to form mature proteins.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The functional genetic units of ARCHAEA.
Deoxyribonucleic acid that makes up the genetic material of archaea.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Diagnostic aid in pancreas function determination.
The genetic complement of an archaeal organism (ARCHAEA) as represented in its DNA.
A genus of extremely thermophilic heterotrophic archaea, in the family THERMOCOCCACEAE, occurring in heated sea flows. They are anaerobic chemoorganotropic sulfidogens.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.
The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An RNA-containing enzyme that plays an essential role in tRNA processing by catalyzing the endonucleolytic cleavage of TRANSFER RNA precursors. It removes the extra 5'-nucleotides from tRNA precursors to generate mature tRNA molecules.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Proteins prepared by recombinant DNA technology.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from Pyrococcus horikoshii. (1/154)

Pyrococcus horikoshii is an obligate anaerobic hyperthermophilic archaeon. In P. horikoshii cells, a hydroperoxide reductase homologue ORF (PH1217) was found to be induced by oxygen. The recombinant protein, which was expressed in E. coli under aerobic conditions, exhibited no activity. However, the recombinant protein prepared under semi-anaerobic conditions exhibited alkyl hydroperoxide reductase activity. Furthermore, it was clarified that it was coupled with the thioredoxin-like system in P. horikoshii. Western blot analysis revealed that the protein was induced by oxygen and hydrogen peroxide. This protein seems to be sensitive to oxygen but forms a thioredoxin-dependent system to eliminate reactive oxygen species in P. horikoshii.  (+info)

RSEARCH: finding homologs of single structured RNA sequences. (2/154)

BACKGROUND: For many RNA molecules, secondary structure rather than primary sequence is the evolutionarily conserved feature. No programs have yet been published that allow searching a sequence database for homologs of a single RNA molecule on the basis of secondary structure. RESULTS: We have developed a program, RSEARCH, that takes a single RNA sequence with its secondary structure and utilizes a local alignment algorithm to search a database for homologous RNAs. For this purpose, we have developed a series of base pair and single nucleotide substitution matrices for RNA sequences called RIBOSUM matrices. RSEARCH reports the statistical confidence for each hit as well as the structural alignment of the hit. We show several examples in which RSEARCH outperforms the primary sequence search programs BLAST and SSEARCH. The primary drawback of the program is that it is slow. The C code for RSEARCH is freely available from our lab's website. CONCLUSION: RSEARCH outperforms primary sequence programs in finding homologs of structured RNA sequences.  (+info)

Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. (3/154)

We report NMR assignments and solution structure of the 71-residue 30S ribosomal protein S28E from the archaean Pyrococcus horikoshii, target JR19 of the Northeast Structural Genomics Consortium. The structure, determined rapidly with the aid of automated backbone resonance assignment (AutoAssign) and automated structure determination (AutoStructure) software, is characterized by a four-stranded beta-sheet with a classic Greek-key topology and an oligonucleotide/oligosaccharide beta-barrel (OB) fold. The electrostatic surface of S28E exhibits positive and negative patches on opposite sides, the former constituting a putative binding site for RNA. The 13 C-terminal residues of the protein contain a consensus sequence motif constituting the signature of the S28E protein family. Surprisingly, this C-terminal segment is unstructured in solution.  (+info)

An archaebacteria-derived glutamyl-tRNA synthetase and tRNA pair for unnatural amino acid mutagenesis of proteins in Escherichia coli. (4/154)

The addition of novel amino acids to the genetic code of Escherichia coli involves the generation of an aminoacyl-tRNA synthetase and tRNA pair that is 'orthogonal', meaning that it functions independently of the synthetases and tRNAs endogenous to E.coli. The amino acid specificity of the orthogonal synthetase is then modified to charge the corresponding orthogonal tRNA with an unnatural amino acid that is subsequently incorporated into a polypeptide in response to a nonsense or missense codon. Here we report the development of an orthogonal glutamic acid synthetase and tRNA pair. The tRNA is derived from the consensus sequence obtained from a multiple sequence alignment of archaeal tRNA(Glu) sequences. The glutamyl-tRNA synthetase is from the achaebacterium Pyrococcus horikoshii. The new orthogonal pair suppresses amber nonsense codons with an efficiency roughly comparable to that of the orthogonal tyrosine pair derived from Methanococcus jannaschii, which has been used to selectively incorporate a variety of unnatural amino acids into proteins in E.coli. Development of the glutamic acid orthogonal pair increases the potential diversity of unnatural amino acid structures that may be incorporated into proteins in E.coli.  (+info)

Crystal structure of the hyperthermophilic inorganic pyrophosphatase from the archaeon Pyrococcus horikoshii. (5/154)

A homolog to the eubacteria inorganic pyrophosphatase (PPase, EC 3.6.1.1) was found in the genome of the hyperthermophilic archaeon Pyrococcus horikoshii. This inorganic pyrophosphatase (Pho-PPase) grows optimally at 88 degrees C. To understand the structural basis for the thermostability of Pho-PPase, we have determined the crystal structure to 2.66 A resolution. The crystallographic asymmetric unit contains three monomers related by approximate threefold symmetry, and a hexamer is built up by twofold crystallographic symmetry. The main-chain fold of Pho-PPase is almost identical to that of the known crystal structure of the model from Sulfolobus acidocaldarius. A detailed comparison of the crystal structure of Pho-PPase with related structures from S. acidocaldarius, Thermus thermophilus, and Escherichia coli shows significant differences that may account for the difference in their thermostabilities. A reduction in thermolabile residues, additional aromatic residues, and more intimate association between subunits all contribute to the larger thermophilicity of Pho-PPase. In particular, deletions in two loops surrounding the active site help to stabilize its conformation, while ion-pair networks unique to Pho-PPase are located in the active site and near the C-terminus. The identification of structural features that make PPases more adaptable to extreme temperature should prove helpful for future biotechnology applications.  (+info)

A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor. (6/154)

Family D DNA polymerase (PolD) is a new type of DNA polymerase possessing polymerization and 3'-5' exonuclease activities. Here we report the characterization of the nuclease activity of PolD from Pyrococcus horikoshii. By site-directed mutagenesis, we verified that the putative Mre11-like nuclease domain in the small subunit (DP1), predicted according to computer analysis and structure inference reported previously, is the catalytic domain. We show that D363, H365 and H454 are the essential residues, while D407, N453, H500, H563 and H565 are critical residues for the activity. We provide experimental evidence demonstrating that manganese, rather than magnesium, is the preferable metal ion for the nuclease activity of PolD. We also show that DP1 alone is insufficient to perform full catalysis, which additionally requires the formation of the PolD complex and manganese ion. We found that a 21 amino acid, subunit-interacting peptide of the sequence from cysteine cluster II of the large subunit (DP2) stimulates the exonuclease activity of DP1 and the internal deletion mutants of PolD lacking the 21-aa sequence. This indicates that the putative zinc finger motif of the cysteine cluster II is deeply involved in the nucleolytic catalysis.  (+info)

Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA. (7/154)

CutA is a small protein that appears to be involved in the mechanism of divalent metal cation tolerance in microorganisms. Here we report the crystal structure of Pyrococcus horikoshii CutA (PhoCutA), with and without Cu(2+), and its metal-binding properties. Crystallographic analyses revealed that PhoCutA forms a stable trimeric structure with intertwined antiparallel beta-strands. The crystal structure of the Cu(2+)-PhoCutA complex shows that the Cu(2+) is located at a trimer-trimer interface and is recognized by the side chains of one Asp(48) from each trimer. In an in vitro experiment, PhoCutA bound to several heavy metals, most of which led to reversible aggregation of the protein; i.e. the aggregates could be completely solubilized by addition of ethylenediamine tetraacetic acid (EDTA) or dialysis against metal free buffer. Substitution of Asp(48) with Ala led to a decrease in the amount of aggregates, suggesting the significant contribution of Asp(48) to the reversible aggregation. To the best of our knowledge, this is the first report which provides the structural evidence for heavy metal-induced multimerization of a protein.  (+info)

Aromatic residues located close to the active center are essential for the catalytic reaction of flap endonuclease-1 from hyperthermophilic archaeon Pyrococcus horikoshii. (8/154)

Flap endonuclease-1 (FEN-1) possessing 5'-flap endonuclease and 5'-->3' exonuclease activity plays important roles in DNA replication and repair. In this study, the kinetic parameters of mutants at highly conserved aromatic residues, Tyr33, Phe35, Phe79, and Phe278-Phe279, in the vicinity of the catalytic centers of FEN-1 were examined. The substitution of these aromatic residues with alanine led to a large reduction in kcat values, although these mutants retained Km values similar to that of the wild-type enzyme. Notably, the kcat of Y33A and F79A decreased 333-fold and 71-fold, respectively, compared with that of the wild-type enzyme. The aromatic residues Tyr33 and Phe79, and the aromatic cluster Phe278-Phe279 mainly contributed to the recognition of the substrates without the 3' projection of the upstream strand (the nick, 5'-recess-end, single-flap, and pseudo-Y substrates) for the both exo- and endo-activities, but played minor roles in recognizing the substrates with the 3' projection (the double flap substrate and the nick substrate with the 3' projection). The replacement of Tyr33, Phe79, and Phe278-Phe279, with non-charged aromatic residues, but not with aliphatic hydrophobic residues, recovered the kcat values almost fully for the substrates without the 3' projection of the upstream strand, suggesting that the aromatic groups of Tyr33, Phe79, and Phe278-Phe279 might be involved in the catalytic reaction, probably via multiple stacking interactions with nucleotide bases. The stacking interactions of Tyr33 and Phe79 might play important roles in fixing the template strand and the downstream strand, respectively, in close proximity to the active center to achieve the productive transient state leading to the hydrolysis.  (+info)

I apologize for any confusion, but "Pyrococcus horikoshii" is not a medical term or concept. It is actually the name of a species of archaea, which are single-celled microorganisms that share some characteristics with both bacteria and eukaryotes (complex cells like those found in animals, plants, and fungi).

"Pyrococcus horikoshii" is particularly notable for its ability to thrive in extremely high temperature environments, with an optimum growth temperature of around 100 degrees Celsius. It was first isolated from a marine volcanic hot spring near Kuroshio, Japan. This organism has been studied extensively in the field of molecular biology and genetics due to its unique properties and potential applications in biotechnology.

"Pyrococcus" is not a medical term, but rather a genus of archaea (single-celled microorganisms) that are extremophiles, meaning they thrive in extreme environments. The name "Pyrococcus" comes from the Greek words "pyr" meaning fire and "kokkos" meaning berry, which refers to their ability to grow at very high temperatures, up to 105 degrees Celsius. These microorganisms are often found in hydrothermal vents and deep-sea sediments. They have potential applications in biotechnology due to their heat-stable enzymes.

"Pyrococcus furiosus" is not a medical term, but a scientific name for an extremophilic archaea species. It's a type of microorganism that thrives in extreme environments, particularly high temperature and acidity. "Pyrococcus furiosus" was first isolated from a marine volcanic vent and has since been studied extensively due to its unique biological properties.

In terms of scientific definition:

"Pyrococcus furiosus" is a species of archaea belonging to the order Thermococcales, family Pyrococcaceae. It's a hyperthermophilic organism, with an optimum growth temperature of around 100°C (212°F), and can survive in temperatures up to 106°C (223°F). The cells are irregularly coccoid, about 0.8-1.5 µm in diameter, and occur singly or in pairs.

The organism obtains energy by fermenting peptides and carbohydrates, producing hydrogen, carbon dioxide, and acetate as end products. "Pyrococcus furiosus" has been used as a model system for studying the biochemistry of archaea and extremophiles, including enzymes that function optimally at high temperatures.

Archaeal proteins are proteins that are encoded by the genes found in archaea, a domain of single-celled microorganisms. These proteins are crucial for various cellular functions and structures in archaea, which are adapted to survive in extreme environments such as high temperatures, high salt concentrations, and low pH levels.

Archaeal proteins share similarities with both bacterial and eukaryotic proteins, but they also have unique features that distinguish them from each other. For example, many archaeal proteins contain unusual amino acids or modifications that are not commonly found in other organisms. Additionally, the three-dimensional structures of some archaeal proteins are distinct from their bacterial and eukaryotic counterparts.

Studying archaeal proteins is important for understanding the biology of these unique organisms and for gaining insights into the evolution of life on Earth. Furthermore, because some archaea can survive in extreme environments, their proteins may have properties that make them useful in industrial and medical applications.

I apologize for any confusion, but "Pyrococcus abyssi" is not a medical term or concept. It is actually the scientific name of an organism, specifically a species of archaea (single-celled microorganisms).

"Pyrococcus abyssi" is a hyperthermophilic archaeon, first isolated from a deep-sea hydrothermal vent, that grows optimally at a temperature of around 98°C. This organism has great biotechnological potential due to its ability to produce various enzymes that function optimally under extreme conditions.

I hope this clarifies any confusion. If you have any further questions or concerns about biology, microbiology, or other scientific topics, please don't hesitate to ask!

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Archaeal RNA refers to the Ribonucleic acid (RNA) molecules that are present in archaea, which are a domain of single-celled microorganisms. RNA is a nucleic acid that plays a crucial role in various biological processes, such as protein synthesis, gene expression, and regulation of cellular activities.

Archaeal RNAs can be categorized into different types based on their functions, including:

1. Messenger RNA (mRNA): It carries genetic information from DNA to the ribosome, where it is translated into proteins.
2. Transfer RNA (tRNA): It helps in translating the genetic code present in mRNA into specific amino acids during protein synthesis.
3. Ribosomal RNA (rRNA): It is a structural and functional component of ribosomes, where protein synthesis occurs.
4. Non-coding RNA: These are RNAs that do not code for proteins but have regulatory functions in gene expression and other cellular processes.

Archaeal RNAs share similarities with both bacterial and eukaryotic RNAs, but they also possess unique features that distinguish them from the other two domains of life. For example, archaeal rRNAs contain unique sequence motifs and secondary structures that are not found in bacteria or eukaryotes. These differences suggest that archaeal RNAs have evolved to adapt to the extreme environments where many archaea live.

Overall, understanding the structure, function, and evolution of archaeal RNA is essential for gaining insights into the biology of these unique microorganisms and their roles in various cellular processes.

"Extein" is not a standard medical term, but it is sometimes used in the field of molecular biology and genetics to refer to the regions of a protein that are located outside of an inserted sequence. The term "extein" is derived from "external" and "protein," and it is often used in contrast to the term "intein," which refers to an internal protein sequence that has the ability to excise itself and join the remaining extein sequences together.

In other words, exteins are the parts of a protein that flank an intein and remain after the intein has been removed during the process of protein splicing. The extein sequences can be joined together by a peptide bond to form a continuous polypeptide chain. This process is important for the proper folding and function of many proteins, particularly those that contain multiple domains or functional units.

It's worth noting that not all proteins contain inteins or exteins, as these features are relatively rare in nature. However, when they do occur, they can provide valuable insights into the evolution and function of proteins, as well as the mechanisms of protein splicing and modification.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

I'm happy to help! However, I believe there might be a slight mistake in your question. "Archaeal" is not a term used to describe genes but rather a group of single-celled organisms that are classified as archaea.

Archaea are one of the three domains of life, along with bacteria and eukaryotes (which include plants, animals, and fungi). Archaea are unique because they share characteristics with both bacteria and eukaryotes, but they also have many features that are distinctly their own. For example, archaea have a different cell membrane structure than bacteria and eukaryotes, which allows them to thrive in extreme environments such as hot springs, salt mines, and deep-sea vents.

Genes, on the other hand, are segments of DNA that contain the instructions for making proteins or performing other important functions in an organism's cells. All living organisms, including archaea, have genes that are passed down from generation to generation. Archaeal genes are made up of the same four nucleotides (A, T, C, and G) as bacterial and eukaryotic genes, and they code for proteins and RNA molecules that are essential for the survival and reproduction of archaea.

So, to summarize, there is no specific definition for "Archaeal genes" because "archaeal" is not a term used to describe genes. However, we can say that archaeal genes are segments of DNA that contain the instructions for making proteins and performing other important functions in archaea.

Archaeal DNA refers to the genetic material present in archaea, a domain of single-celled microorganisms lacking a nucleus. Like bacteria, archaea have a single circular chromosome that contains their genetic information. However, archaeal DNA is significantly different from bacterial and eukaryotic DNA in terms of its structure and composition.

Archaeal DNA is characterized by the presence of unique modifications such as methylation patterns, which help distinguish it from other types of DNA. Additionally, archaea have a distinct set of genes involved in DNA replication, repair, and recombination, many of which are more similar to those found in eukaryotes than bacteria.

One notable feature of archaeal DNA is its resistance to environmental stressors such as extreme temperatures, pH levels, and salt concentrations. This allows archaea to thrive in some of the most inhospitable environments on Earth, including hydrothermal vents, acidic hot springs, and highly saline lakes.

Overall, the study of archaeal DNA has provided valuable insights into the evolutionary history of life on Earth and the unique adaptations that allow these organisms to survive in extreme conditions.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Selenomethionine is an organic form of selenium, which is an essential trace element in human nutrition. It is incorporated into proteins in place of methionine, one of the 20 standard amino acids, and functions as an antioxidant by helping to prevent cellular damage from free radicals. Selenomethionine can be found in a variety of foods, including brazil nuts, fish, meat, and whole grains, and is also available as a dietary supplement.

An archaeal genome refers to the complete set of genetic material or DNA present in an archaea, a single-celled microorganism that is found in some of the most extreme environments on Earth. The genome of an archaea contains all the information necessary for its survival, including the instructions for building proteins and other essential molecules, as well as the regulatory elements that control gene expression.

Archaeal genomes are typically circular in structure and range in size from about 0.5 to over 5 million base pairs. They contain genes that are similar to those found in bacteria and eukaryotes, as well as unique genes that are specific to archaea. The study of archaeal genomes has provided valuable insights into the evolutionary history of life on Earth and has helped scientists understand the adaptations that allow these organisms to thrive in such harsh environments.

"Thermococcus" is not a medical term, but rather a genus of archaea (single-celled microorganisms) that are extremophiles, meaning they thrive in extreme environments. Specifically, Thermococcus species are found in hydrothermal vents and other high-temperature, high-pressure, and anaerobic environments. They are known for their ability to grow at very high temperatures, with some species able to grow at temperatures up to 122°C (252°F). These microorganisms play a significant role in the global carbon cycle and have potential applications in biotechnology.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Cellulase is a type of enzyme that breaks down cellulose, which is a complex carbohydrate and the main structural component of plant cell walls. Cellulases are produced by certain bacteria, fungi, and protozoans, and are used in various industrial applications such as biofuel production, food processing, and textile manufacturing. In the human body, there are no known physiological roles for cellulases, as humans do not produce these enzymes and cannot digest cellulose.

X-ray diffraction (XRD) is not strictly a medical definition, but it is a technique commonly used in the field of medical research and diagnostics. XRD is a form of analytical spectroscopy that uses the phenomenon of X-ray diffraction to investigate the crystallographic structure of materials. When a beam of X-rays strikes a crystal, it is scattered in specific directions and with specific intensities that are determined by the arrangement of atoms within the crystal. By measuring these diffraction patterns, researchers can determine the crystal structures of various materials, including biological macromolecules such as proteins and viruses.

In the medical field, XRD is often used to study the structure of drugs and drug candidates, as well as to analyze the composition and structure of tissues and other biological samples. For example, XRD can be used to investigate the crystal structures of calcium phosphate minerals in bone tissue, which can provide insights into the mechanisms of bone formation and disease. Additionally, XRD is sometimes used in the development of new medical imaging techniques, such as phase-contrast X-ray imaging, which has the potential to improve the resolution and contrast of traditional X-ray images.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Ribonuclease P (RNase P) is an endonuclease enzyme complex that is found in all three domains of life: archaea, bacteria, and eukaryotes. Its primary function is to process precursor transfer RNA (tRNA) molecules by cleaving the 5' leader sequence to generate mature tRNAs.

RNase P is unique because it consists of both a protein component and an RNA subunit, known as the RNA moiety or RNA catalytic subunit. In bacteria and archaea, the RNA subunit is primarily responsible for the enzymatic activity, while in eukaryotes, the protein component plays a more significant role.

RNase P's function in tRNA processing is essential for protein synthesis, as mature tRNAs are necessary for decoding messenger RNA (mRNA) sequences and translating them into proteins during translation. Dysregulation or mutations in RNase P can lead to various human diseases, including mitochondrial disorders, neurodevelopmental abnormalities, and cancer.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

Archaea are a domain of single-celled microorganisms that lack membrane-bound nuclei and other organelles. They are characterized by the unique structure of their cell walls, membranes, and ribosomes. Archaea were originally classified as bacteria, but they differ from bacteria in several key ways, including their genetic material and metabolic processes.

Archaea can be found in a wide range of environments, including some of the most extreme habitats on Earth, such as hot springs, deep-sea vents, and highly saline lakes. Some species of Archaea are able to survive in the absence of oxygen, while others require oxygen to live.

Archaea play important roles in global nutrient cycles, including the nitrogen cycle and the carbon cycle. They are also being studied for their potential role in industrial processes, such as the production of biofuels and the treatment of wastewater.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

"Pyrococcus horikoshii" at the Encyclopedia of Life WORMS entry LPSN Type strain of Pyrococcus horikoshii at BacDive - the ... 1998). "Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough". ... Pyrococcus horikoshii is a hyperthermophilic, anaerobic archaeon, first isolated from hydrothermal fluid samples obtained at ... August 2013). "Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation". The Journal of ...
Crystal structure of PH1346 protein from Pyrococcus horikoshii ... Find proteins for O59071 (Pyrococcus horikoshii (strain ATCC ... Crystal structure of Glutamide Amido Transferase from Pyrococcus horikoshii OT3. Lokanath, N.K., Kunishima, N.. To be published ... Crystal structure of PH1346 protein from Pyrococcus horikoshii. *PDB DOI: https://doi.org/10.2210/pdb1WL8/pdb ...
Timeline for Species Pyrococcus horikoshii [TaxId:53953] from c.108.1.10 Phosphoglycolate phosphatase, PGPase: *Species ... called Species Pyrococcus horikoshii [TaxId:70601] from c.108.1.10 Phosphoglycolate phosphatase, PGPase. *Species Pyrococcus ... PDB entry in Species: Pyrococcus horikoshii [TaxId: 53953]:. *Domain(s) for 1wr8: *. Domain d1wr8a_: 1wr8 A: [114836]. ... Lineage for Species: Pyrococcus horikoshii [TaxId: 53953]. *Root: SCOPe 2.08 *. Class c: Alpha and beta proteins (a/b) [51349 ...
Timeline for Species Pyrococcus horikoshii [TaxId:53953] from a.7.12.1 Hypothetical protein PH0236, N-terminal domain: *Species ... PDB entries in Species: Pyrococcus horikoshii [TaxId: 53953]:. *Domain(s) for 1vct: *. Domain d1vcta1: 1vct A:9-107 [119986]. ... Species Pyrococcus horikoshii [TaxId:53953] from a.7.12.1 Hypothetical protein PH0236, N-terminal domain appears in SCOPe 2.07 ... Lineage for Species: Pyrococcus horikoshii [TaxId: 53953]. *Root: SCOPe 2.08 *. Class a: All alpha proteins [46456] (290 folds) ...
Find proteins for O59384 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) ... Crystal structure of PH1733, an aspartate racemase homologue, from pyrococcus horikoshii OT3. Kita, A., Tasaki, S., Yohda, M., ... Crystal structure of PH1733, an aspartate racemase homologue, from Pyrococcus horikoshii OT3. *PDB DOI: https://doi.org/10.2210 ...
Pyrococcus horikoshii OT3). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Pyrococcus horikoshii - PH1633. Organism. Pyrococcus horikoshii. Gene Name. PH1633. Product. 30S ribosomal protein S9. ...
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii OT3 ... Pyrococcus horikoshii OT3. Mutation(s): 0 Gene Names: PH1830, gap. EC: 1.2.1.59. ... Find proteins for O59494 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)) ... Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii OT3. Ito, K., Arai, R., Kamo-Uchikubo ...
CRYSTAL STRUCTURES OF RADA INTEIN FROM PYROCOCCUS HORIKOSHII - 4E2T , canSARS ...
Pyrococcus horikoshii 3qho_c O58925 99.60 1.20E-19 7.70E-24 170.50 0 0 0 0 0 0 0 0 ...
Crystal structure of DNA primase from Pyrococcus horikoshii ... Ito, N. et al., Crystal structure of the Pyrococcus horikoshii ... Crystal structure of DNA primase from Pyrococcus horikoshii Coordinates. PDB Format Method. X-RAY DIFFRACTION 1.80 Å. Oligo ...
Structure of Protease 1 From Pyrococcus Horikoshii Co-Crystallized in Presence of 10 Mm Tb-XO4 and Potassium Iodide. ... The structure of Structure of Protease 1 From Pyrococcus Horikoshii Co-Crystallized in Presence of 10 Mm Tb-XO4 and Potassium ... Iodine binding site 1 out of 11 in the Structure of Protease 1 From Pyrococcus Horikoshii Co-Crystallized in Presence of 10 Mm ... Iodine binding site 2 out of 11 in the Structure of Protease 1 From Pyrococcus Horikoshii Co-Crystallized in Presence of 10 Mm ...
CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3 ... CRYSTAL STRUCTURE OF AROMATIC AMINOTRANSFERASE FROM PYROCOCCUS HORIKOSHII OT3 Coordinates. PDB Format Method. X-RAY DIFFRACTION ... molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii ...
Observation of a calcium-binding site in the γ-class carbonic anhydrase from Pyrococcus horikoshii. ... Structure of a haloacid dehalogenase superfamily phosphatase PH1421 from Pyrococcus horikoshii OT3: oligomeric state and ... Three crystal structures of the γ-carbonic anhydrase enzyme from P. horikoshii were solved in space group F4132. The enzyme ...
Crystal structure of a trimeric exonuclease PhoExo I from Pyrococcus horikoshii OT3 at 2.15A resolution. ... 4yot is a 3 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. ... A structural analysis of PhoExo I, the homologous enzyme from P. horikoshii OT3, showed that PhoExo I utilizes an RNase H-like ... from the hyperthermophilic archaeon Pyrococcus furiosus, which may be involved in the Thermococcales-specific DNA repair system ...
Pyrococcus horikoshii. Primary Citation. Crystal structure of acylphosphatase from hyperthermophilic archaeon Pyrococcus ...
SEKAKELLKGFGSINDFMDAIPKIVSVDDVIER - Pyrococcus horikoshii; DNA primase large subunit MFFFENADILLPPSLIERNVHLWATIFVGAL - output ...
Structural Insights on the New Mechanism of Trehalose Synthesis by Trehalose Synthase Tret from Pyrococcus Horikoshii. ... the enzymes from the thermophilic bacterium Rubrobacter xylanophilus and the hyperthermophilic archaeon Pyrococcus horikoshii ...
Pyrococcus horikoshii OT3. alkyl β-glucosidase (membrane-bound) (BGPh;BglA;PH0366). Last update: 2023-11-16 © Copyright 1998- ...
The closely related archaeal transporters GltPh from Pyrococcus horikoshii and GltTk from Thermococcus kodakarensis of the ... Yernool, D., Boudker, O., Jin, Y. & Gouaux, E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. ... Functional characterization of a Na+-dependent aspartate transporter from Pyrococcus horikoshii. J. Biol. Chem. 284, 17540- ...
hypothetical protein from Pyrococcus horikoshii OT3. 2dt5. Crystal Structure of TTHA1657 (AT-rich DNA-binding protein) from ... Crystal structure of hypothetical protein PH1109 from Pyrococcus horikoshii. 2fp4. Crystal structure of pig GTP-specific ... Conserved hypothetical protein Pfu-723267-001 from Pyrococcus furiosus. 2csu. Crystal structure of PH0766 from Pyrococcus ... hypothetical protein from Pyrococcus horikoshii OT3. 2d5a. ...
... exonuclease PhoExo I from Pyrococcus horikoshii OT3. ... horikoshii OT3 was produced as inclusion bodies in E. coli ...
Pyrococcus horikoshii TET2 peptidase assembling process and associated functional regulation.. Journal of Biological Chemistry ... The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an ... Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii.. Biochemistry ... Studies on the parameters controlling the stability of the TET peptidase superstructure from Pyrococcus horikoshii revealed a ...
2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii Nature 431:811-818. ...
... determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP. Structure 9, 817-826.10.1016/S0969-2126(01) ...
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Protein Sci. 2003 ;12(12):2823-30. ... The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism. Acta ... Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus. Proteins. 2012 ;80(7):1901-6. ...
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Protein Sci. 2003 ;12(12):2823-30. ... Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus. Proteins. 2012 ;80(7):1901-6. ...
Crystal structure of nucleotide diphosphate kinase from Pyrococcus horikoshii. 2dxd. Crystal structure of nucleoside ...
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Pyrococcus horikoshii OT3. 2d2i. Crystal Structure of NADP- ...

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