Structure of Salmonella Effector Protein SopB N-terminal Domain in Complex with Host Rho GTPase Cdc42

被引：20
|
作者：
Burkinshaw, Brianne J.
Prehna, Gerd
Worrall, Liam J.
Strynadka, Natalie C. J. [1 ]
机构：
[1] Univ British Columbia, Dept Biochem & Mol Biol, Life Sci Ctr, Vancouver, BC V6T 1Z3, Canada
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2012年 / 287卷 / 16期
基金：
加拿大自然科学与工程研究理事会;
关键词：
BINDING DOMAIN; GLOBAL BURDEN; TYPHIMURIUM; IDENTIFICATION; PHOSPHATASE; ACTIVATION; REGION;
D O I：
10.1074/jbc.M111.331330
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
SopB is a type III secreted Salmonella effector protein with phosphoinositide phosphatase activity and a distinct GTPase binding domain. The latter interacts with host Cdc42, an essential Rho GTPase that regulates critical events in eukaryotic cytoskeleton organization and membrane trafficking. Structural and biochemical analysis of the SopB GTPase binding domain in complex with Cdc42 shows for the first time that SopB structurally and functionally mimics a host guanine nucleotide dissociation inhibitor (GDI) by contacting key residues in the regulatory switch regions of Cdc42 and slowing Cdc42 nucleotide exchange.
引用
收藏
页码：13348 / 13355
页数：8
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