2vq2

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

spinqualitylabelsall models 2vq2, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vq2 is a 1 chain structure with sequence from "diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, GOL, MG, SO3, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structure of a widely conserved type IV pilus biogenesis factor that affects the stability of secretin multimers.,Trindade MB, Job V, Contreras-Martel C, Pelicic V, Dessen A J Mol Biol. 2008 May 16;378(5):1031-9. Epub 2008 Mar 19. PMID:18433773 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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