2VQ2: Crystal structure of PilW, widely conserved type IV pilus biogenesis factor

Citation:
Abstract
Type IV pili (Tfp) are arguably the most widespread pili in bacteria, whose biogenesis requires a complex machinery composed of as many as 18 different proteins. This includes the conserved outer membrane-localized secretin, which forms a pore through which Tfp emerge on the bacterial surface. Although, in most model species studied, secretin oligomerization and functionality requires the action of partner lipoproteins, structural information regarding these molecules is limited. We report the high-resolution crystal structure of PilW, the partner lipoprotein of the type IV pilus secretin PilQ from Neisseria meningitidis, which defines a conserved class of Tfp biogenesis proteins involved in the formation and/or stability of secretin multimers in a wide variety of bacteria. The use of the PilW structure as a blueprint reveals an area of high-level sequence conservation in homologous proteins from different pathogens that could reflect a possible secretin-binding site. These results could be exploited for the development of new broad-spectrum antibacterials interfering with the biogenesis of a widespread virulence factor.
PDB ID: 2VQ2Download
MMDB ID: 64650
PDB Deposition Date: 2008/3/10
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 1.54  Å
Source Organism:
Similar Structures:
Biological Unit for 2VQ2: dimeric; determined by author and by software (PQS)
Molecular Components in 2VQ2
Label Count Molecule
Proteins (2 molecules)
2
Putative Fimbrial Biogenesis and Twitching Motility Protein
Molecule annotation
Chemicals (14 molecules)
1
2
2
2
3
6
4
2
5
2
* Click molecule labels to explore molecular sequence information.

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