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结构和功能研究表明,EPEC 效应蛋白 EspG 可直接结合 p21 激活激酶。

Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase.

机构信息

Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.

出版信息

Biochemistry. 2011 Feb 15;50(6):917-9. doi: 10.1021/bi1020138. Epub 2011 Jan 24.

Abstract

Bacterial pathogens secrete effectors into their hosts that subvert host defenses and redirect host processes. EspG is a type three secretion effector with a disputed function that is found in enteropathogenic Escherichia coli. Here we show that EspG is structurally similar to VirA, a Shigella virulence factor; EspG has a large, conserved pocket on its surface; EspG binds directly to the amino-terminal inhibitory domain of human p21-activated kinase (PAK); and mutations to conserved residues in the surface pocket disrupt the interaction with PAK.

摘要

细菌病原体将效应物分泌到宿主中,颠覆宿主防御并重新引导宿主进程。EspG 是一种三型分泌效应物,其功能存在争议,存在于肠致病性大肠杆菌中。在这里,我们表明 EspG 在结构上与志贺氏菌毒力因子 VirA 相似;EspG 表面有一个大的、保守的口袋;EspG 直接结合人 P21 激活激酶 (PAK) 的氨基末端抑制结构域;并且表面口袋中保守残基的突变会破坏与 PAK 的相互作用。

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