2VQ2

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

2VQ2 の概要

• エントリーDOI: 10.2210/pdb2vq2/pdb
• 分子名称: PUTATIVE FIMBRIAL BIOGENESIS AND TWITCHING MOTILITY PROTEIN, SULFATE ION, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: secretin, tpr repeat, type iv pilus, bacterail virulence, structural protein
• 由来する生物種: NEISSERIA MENINGITIDIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25774.49

構造登録者

Trinidade, M.B.,Job, V.,Contreras-Martel, C.,Pelicic, V.,Dessen, A. (登録日: 2008-03-10, 公開日: 2008-05-27, 最終更新日: 2024-10-16)

主引用文献

Trindade, M.B.,Job, V.,Contreras-Martel, C.,Pelicic, V.,Dessen, A.
Structure of a widely conserved type IV pilus biogenesis factor that affects the stability of secretin multimers.
J. Mol. Biol., 378:1031-1039, 2008

PubMed 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.

PubMed: 18433773
DOI: 10.1016/j.jmb.2008.03.028

実験手法

X-RAY DIFFRACTION (1.54 Å)