5KEW

Vibrio parahaemolyticus VtrA/VtrC complex bound to the bile salt taurodeoxycholate

5KEW の概要

• エントリーDOI: 10.2210/pdb5kew/pdb
• 関連するPDBエントリー: 5KEV
• 分子名称: VtrA Protein, VtrC Protein, Taurodeoxycholate, ... (7 entities in total)
• 機能のキーワード: heterodimer, alpha/beta, calycin beta barrel superfamily, bile salt receptor, taurodeoxycholate, signaling protein
• 由来する生物種: Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 86363.06

構造登録者

Tomchick, D.R.,Orth, K.,Rivera-Cancel, G. (登録日: 2016-06-10, 公開日: 2016-07-20, 最終更新日: 2024-03-06)

主引用文献

Li, P.,Rivera-Cancel, G.,Kinch, L.N.,Salomon, D.,Tomchick, D.R.,Grishin, N.V.,Orth, K.
Bile salt receptor complex activates a pathogenic type III secretion system.
Elife, 5:-, 2016

PubMed Abstract: Bile is an important component of the human gastrointestinal tract with an essential role in food absorption and antimicrobial activities. Enteric bacterial pathogens have developed strategies to sense bile as an environmental cue to regulate virulence genes during infection. We discovered that Vibrio parahaemolyticus VtrC, along with VtrA and VtrB, are required for activating the virulence type III secretion system 2 in response to bile salts. The VtrA/VtrC complex activates VtrB in the presence of bile salts. The crystal structure of the periplasmic domains of the VtrA/VtrC heterodimer reveals a β-barrel with a hydrophobic inner chamber. A co-crystal structure of VtrA/VtrC with bile salt, along with biophysical and mutational analysis, demonstrates that the hydrophobic chamber binds bile salts and activates the virulence network. As part of a family of conserved signaling receptors, VtrA/VtrC provides structural and functional insights into the evolutionarily conserved mechanism used by bacteria to sense their environment.

PubMed: 27377244
DOI: 10.7554/eLife.15718

実験手法

X-RAY DIFFRACTION (2.103 Å)