4EOB

Structure of the type VI peptidoglycan amidase effector Tse1 from Pseudomonas aeruginosa

4EOB の概要

• エントリーDOI: 10.2210/pdb4eob/pdb
• 分子名称: type VI amidase effector Tse1 (2 entities in total)
• 機能のキーワード: amidase, hydrolase, protease, bacteriolytic, peptidoglycan degrading, tsi1, pa1845
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 70119.31

構造登録者

Chou, S.,Mougous, J.D. (登録日: 2012-04-13, 公開日: 2012-05-30, 最終更新日: 2024-10-16)

主引用文献

Chou, S.,Bui, N.K.,Russell, A.B.,Lexa, K.W.,Gardiner, T.E.,LeRoux, M.,Vollmer, W.,Mougous, J.D.
Structure of a peptidoglycan amidase effector targeted to Gram-negative bacteria by the type VI secretion system.
Cell Rep, 1:656-664, 2012

PubMed Abstract: The target range of a bacterial secretion system can be defined by effector substrate specificity or by the efficacy of effector delivery. Here, we report the crystal structure of Tse1, a type VI secretion (T6S) bacteriolytic amidase effector from Pseudomonas aeruginosa. Consistent with its role as a toxin, Tse1 has a more accessible active site than related housekeeping enzymes. The activity of Tse1 against isolated peptidoglycan shows its capacity to act broadly against Gram-negative bacteria and even certain Gram-positive species. Studies with intact cells indicate that Gram-positive bacteria can remain vulnerable to Tse1 despite cell wall modifications. However, interbacterial competition studies demonstrate that Tse1-dependent lysis is restricted to Gram-negative targets. We propose that the previously observed specificity for T6S against Gram-negative bacteria is a consequence of high local effector concentration achieved by T6S-dependent targeting to its site of action rather than inherent effector substrate specificity.

PubMed: 22813741
DOI: 10.1016/j.celrep.2012.05.016

実験手法

X-RAY DIFFRACTION (2.611 Å)