Cryo-EM of the injectisome and type III secretion systems
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Cryo-EM of the injectisome and type III secretion systems. / Bergeron, Julien R C; Marlovits, Thomas C.
in: CURR OPIN STRUC BIOL, Jahrgang 75, 102403, 08.2022.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung
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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 -