5VTM

The crystal structure of minor pseudopilin ternary complex of XcpVWX from the Type 2 secretion system of Pseudomonas aeruginosa

5VTM の概要

• エントリーDOI: 10.2210/pdb5vtm/pdb
• 分子名称: Type II secretion system protein J, Type II secretion system protein K, Type II secretion system protein I, ... (5 entities in total)
• 機能のキーワード: type 2 secretion system, transport protein
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 63562.19

構造登録者

Zhang, Y.,Jia, Z. (登録日: 2017-05-17, 公開日: 2018-05-23, 最終更新日: 2024-11-20)

主引用文献

Zhang, Y.,Faucher, F.,Zhang, W.,Wang, S.,Neville, N.,Poole, K.,Zheng, J.,Jia, Z.
Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.
PLoS Pathog., 14:e1007343-e1007343, 2018

PubMed Abstract: Pseudomonas aeruginosa utilizes the Type II secretion system (T2SS) to translocate a wide range of large, structured protein virulence factors through the periplasm to the extracellular environment for infection. In the T2SS, five pseudopilins assemble into the pseudopilus that acts as a piston to extrude exoproteins out of cells. Through structure determination of the pseudopilin complexes of XcpVWX and XcpVW and function analysis, we have confirmed that two minor pseudopilins, XcpV and XcpW, constitute a core complex indispensable to the pseudopilus tip. The absence of either XcpV or -W resulted in the non-functional T2SS. Our small-angle X-ray scattering experiment for the first time revealed the architecture of the entire pseudopilus tip and established the working model. Based on the interaction interface of complexes, we have developed inhibitory peptides. The structure-based peptides not only disrupted of the XcpVW core complex and the entire pseudopilus tip in vitro but also inhibited the T2SS in vivo. More importantly, these peptides effectively reduced the virulence of P. aeruginosa towards Caenorhabditis elegans.

PubMed: 30346996
DOI: 10.1371/journal.ppat.1007343

実験手法

X-RAY DIFFRACTION (2.041 Å)