Cryo-EM of the injectisome and type III secretion systems

TY - JOUR

T1 - Cryo-EM of the injectisome and type III secretion systems

AU - Bergeron, Julien R C

AU - Marlovits, Thomas C

N1 - Copyright © 2022 The Author(s). Published by Elsevier Ltd.. All rights reserved.

PY - 2022/8

Y1 - 2022/8

N2 - Double-membrane-spanning protein complexes, such as the T3SS, had long presented an intractable challenge for structural biology. As a consequence, until a few years ago, our molecular understanding of this fascinating complex was limited to composite models, consisting of structures of isolated domains, positioned within the overall complex. Most of the membrane-embedded components remained completely uncharacterized. In recent years, the emergence of cryo-electron microscopy (cryo-EM) as a method for determining protein structures to high resolution, has be transformative to our capacity to understand the architecture of this complex, and its mechanism of substrate transport. In this review, we summarize the recent structures of the various T3SS components, determined by cryo-EM, and highlight the regions of the complex that remain to be characterized. We also discuss the recent structural insights into the mechanism of effector transport through the T3SS. Finally, we highlight some of the challenges that remain to be tackled.

AB - Double-membrane-spanning protein complexes, such as the T3SS, had long presented an intractable challenge for structural biology. As a consequence, until a few years ago, our molecular understanding of this fascinating complex was limited to composite models, consisting of structures of isolated domains, positioned within the overall complex. Most of the membrane-embedded components remained completely uncharacterized. In recent years, the emergence of cryo-electron microscopy (cryo-EM) as a method for determining protein structures to high resolution, has be transformative to our capacity to understand the architecture of this complex, and its mechanism of substrate transport. In this review, we summarize the recent structures of the various T3SS components, determined by cryo-EM, and highlight the regions of the complex that remain to be characterized. We also discuss the recent structural insights into the mechanism of effector transport through the T3SS. Finally, we highlight some of the challenges that remain to be tackled.

U2 - 10.1016/j.sbi.2022.102403

DO - 10.1016/j.sbi.2022.102403

M3 - SCORING: Review article

C2 - 35724552

VL - 75

JO - CURR OPIN STRUC BIOL

JF - CURR OPIN STRUC BIOL

SN - 0959-440X

M1 - 102403

ER -