7K08

Cryo-EM structure of the nonameric EscV cytosolic domain from the type III secretion system

7K08 の概要

• エントリーDOI: 10.2210/pdb7k08/pdb
• EMDBエントリー: 22589 22590
• 分子名称: Translocator EscV (1 entity in total)
• 機能のキーワード: injectisome, nonamer, export apparatus, secretion, protein transport
• 由来する生物種: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 351734.70

構造登録者

Majewski, D.D.,Lyons, B.J.E.,Atkinson, C.E.,Strynadka, N.C.J. (登録日: 2020-09-03, 公開日: 2020-11-25, 最終更新日: 2024-03-06)

主引用文献

Majewski, D.D.,Lyons, B.J.E.,Atkinson, C.E.,Strynadka, N.C.J.
Cryo-EM analysis of the SctV cytosolic domain from the enteropathogenic E. coli T3SS injectisome.
J.Struct.Biol., 212:107660-107660, 2020

PubMed 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 (SctV) from the enteropathogenic Escherichia coli injectisome. SctV forms a nonameric ring with primarily electrostatic interactions between its subunits. Molecular dynamics simulations show that monomeric SctV 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.

PubMed: 33129970
DOI: 10.1016/j.jsb.2020.107660

実験手法

ELECTRON MICROSCOPY (4.7 Å)