3VPJ

crystal structure of type VI effector Tse1 from Pseudomonas aeruginosa in complex with immune protein Tsi1

3VPJ の概要

• エントリーDOI: 10.2210/pdb3vpj/pdb
• 関連するPDBエントリー: 3VPI
• 分子名称: type VI secretion exported 1, Tse1-specific immunity protein (3 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 158317.52

構造登録者

Ding, J.,Wang, W.,Wang, D.C. (登録日: 2012-03-04, 公開日: 2012-06-27, 最終更新日: 2024-11-20)

主引用文献

Ding, J.,Wang, W.,Feng, H.,Zhang, Y.,Wang, D.C.
Structural insights into the Pseudomonas aeruginosa type VI virulence effector Tse1 bacteriolysis and self-protection mechanisms
J.Biol.Chem., 287:26911-26920, 2012

PubMed Abstract: Recently, it was identified that Pseudomonas aeruginosa competes with rival cells to gain a growth advantage using a novel mechanism that includes two interrelated processes as follows: employing type VI secretion system (T6SS) virulence effectors to lyse other bacteria, and at the same time producing specialized immunity proteins to inactivate their cognate effectors for self-protection against mutual toxicity. To explore the structural basis of these processes in the context of functional performance, the crystal structures of the T6SS virulence effector Tse1 and its complex with the corresponding immunity protein Tsi1 were determined, which, in association with mutagenesis and Biacore analyses, provided a molecular platform to resolve the relevant structural questions. The results indicated that Tse1 features a papain-like structure and conserved catalytic site with distinct substrate-binding sites to hydrolyze its murein peptide substrate. The immunity protein Tsi1 interacts with Tse1 via a unique interactive recognition mode to shield Tse1 from its physiological substrate. These findings reveal both the structural mechanisms for bacteriolysis and the self-protection against the T6SS effector Tse1. These mechanisms are significant not only by contributing to a novel understanding of niche competition among bacteria but also in providing a structural basis for antibacterial agent design and the development of new strategies to fight P. aeruginosa.

PubMed: 22700987
DOI: 10.1074/jbc.M112.368043

実験手法

X-RAY DIFFRACTION (2.5 Å)