• Despite a wealth of other structural and biochemical information, little is known about how pilus formation is orchestrated at the bacterial cell surface. (esrf.fr)
  • We present here a crystal structure capturing the pilus assembly platform in the act of secreting its cognate substrate. (esrf.fr)
  • We have recently solved a new crystal structure describing the first step in pilus biogenesis - the FimD usher bound to its cognate FimC:FimH substrate - using diffraction data collected at beamline ID23-1 ( Figure 107 ). (esrf.fr)
  • Two black lines indicate the position of the usher within the bacterial outer-membrane. (esrf.fr)
  • Fig. 107: Crystal structure of the FimD:FimC:FimH complex shown as side view and ribbon/surface representation. (esrf.fr)
  • A striking feature of the active usher conformation is that the FimC:FimH complex is bound to a newly identified site on the C-terminal domains (CTDs) of FimD. (esrf.fr)
  • a) The FimD:FimC:FimH complex. (esrf.fr)
  • In the described conformation, the FimD NTD is in an ideal position for the recruitment of the next chaperone:subunit complex FimC':FimG. (esrf.fr)
  • From there, he worked with Markus Grütter at the University of Zurich, elucidating the structures of numerous proteins. (psi.ch)
  • We are interested in protein structure both from a structure determination and from a structural bioinformatics perspective, which means obtaining high resolution "bioimages" of proteins and extracting as much information as possible from them. (psi.ch)
  • Citrullination is a unique type of PTM that is catalysed by peptidylarginine deiminase (PAD) enzymes, which regulate a multitude of physiological functions such as apoptosis, gene expression and immune response by altering the structure and function of cellular proteins. (bvsalud.org)
  • Along with the crystal structure of the closed state of the FimD pore domain, this structure sheds new light on the mechanism of usher activation. (esrf.fr)
  • We are studying protein structures and crystal lattices by employing a variety of approaches, in particular concepts from the field of molecular evolution. (psi.ch)
  • We have demonstrated that this approach can be successfully applied to address the problem of distinguishing, in a crystal structure, the biologically relevant interface(s) from those that are merely lattice contacts (reviewed in Capitani et al. (psi.ch)
  • The chaperone:subunit complexes are then targeted differentially to the usher FimD, which catalyses their assembly. (esrf.fr)
  • This structure, solved at 2.8 Å resolution, shows the full-length usher FimD in its active state. (esrf.fr)
  • The usher FimD comprises 5 domains: the N-terminal domain (NTD), the C-terminal domains (CTD1 and CTD2), the plug domain and the β-barrel pore domain. (esrf.fr)
  • Fig. 108: Structural model of the subunit incorporation cycle at the FimD usher, represented as in Figure 107 . (esrf.fr)
  • Uropathogenic Escherichia coli (UPEC) attach specifically to human bladder cells using surface structures known as type 1 pili. (esrf.fr)
  • Notable structures include thioredoxin structures, glutamate decarboxylase, and bacterial type 1 pili. (psi.ch)
  • It represents a very interesting system to study hybrid approaches to structure determination and structure-function relationships. (psi.ch)
  • Here, we reconstituted the entire type 1 pilus rod assembly reaction in vitro, using all constituent protein subunits in the presence of the assembly platform FimD, and identified the so-far uncharacterized subunit FimI as an irreversible assembly terminator. (nih.gov)