Cryo-EM analysis of the SctV cytosolic domain from the enteropathogenic E. coli T3SS injectisome.

Abstract:

:The bacterial injectisome and flagella both rely on type III secretion systems for their assembly. The syringe-like injectisome creates a continuous channel between the bacterium and the host cell, through which signal-modulating effector proteins are secreted. The inner membrane pore protein SctV controls the hierarchy of substrate selection and may also be involved in energizing secretion. We present the 4.7 Å cryo-EM structure of the SctV cytosolic domain (SctVC) from the enteropathogenic Escherichia coli injectisome. SctVC forms a nonameric ring with primarily electrostatic interactions between its subunits. Molecular dynamics simulations show that monomeric SctVC maintains a closed conformation, in contrast with previous studies on flagellar homologue FlhA. Comparison with substrate-bound homologues suggest that a conformational change would be required to accommodate binding partners.

journal_name

J Struct Biol

authors

Majewski DD,Lyons BJE,Atkinson CE,Strynadka NCJ

doi

10.1016/j.jsb.2020.107660

subject

Has Abstract

pub_date

2020-12-01 00:00:00

pages

107660

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(20)30233-1

journal_volume

212

pub_type

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