Structural basis of torque generation in the bi-directional bacterial flagellar motor

Research output: Contribution to journal › Review › Research › peer-review

Standard

Structural basis of torque generation in the bi-directional bacterial flagellar motor. / Hu, Haidai; Santiveri, Mònica; Wadhwa, Navish; Berg, Howard C; Erhardt, Marc; Taylor, Nicholas M.I.

In: Trends in Biochemical Sciences, Vol. 47, No. 2, 2022, p. 160-172.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Hu, H, Santiveri, M, Wadhwa, N, Berg, HC, Erhardt, M & Taylor, NMI 2022, 'Structural basis of torque generation in the bi-directional bacterial flagellar motor', Trends in Biochemical Sciences, vol. 47, no. 2, pp. 160-172. https://doi.org/10.1016/j.tibs.2021.06.005

APA

Hu, H., Santiveri, M., Wadhwa, N., Berg, H. C., Erhardt, M., & Taylor, N. M. I. (2022). Structural basis of torque generation in the bi-directional bacterial flagellar motor. Trends in Biochemical Sciences, 47(2), 160-172. https://doi.org/10.1016/j.tibs.2021.06.005

Vancouver

Hu H, Santiveri M, Wadhwa N, Berg HC, Erhardt M, Taylor NMI. Structural basis of torque generation in the bi-directional bacterial flagellar motor. Trends in Biochemical Sciences. 2022;47(2):160-172. https://doi.org/10.1016/j.tibs.2021.06.005

Author

Hu, Haidai ; Santiveri, Mònica ; Wadhwa, Navish ; Berg, Howard C ; Erhardt, Marc ; Taylor, Nicholas M.I. / Structural basis of torque generation in the bi-directional bacterial flagellar motor. In: Trends in Biochemical Sciences. 2022 ; Vol. 47, No. 2. pp. 160-172.

Bibtex

@article{1be42cfe1c91471584e16577039a229c,
title = "Structural basis of torque generation in the bi-directional bacterial flagellar motor",
abstract = "The flagellar stator unit is an oligomeric complex of two membrane proteins (MotA5B2) that powers bi-directional rotation of the bacterial flagellum. Harnessing the ion motive force across the cytoplasmic membrane, the stator unit operates as a miniature rotary motor itself to provide torque for rotation of the flagellum. Recent cryo-electron microscopic (cryo-EM) structures of the stator unit provided novel insights into its assembly, function, and subunit stoichiometry, revealing the ion flux pathway and the torque generation mechanism. Furthermore, in situ cryo-electron tomography (cryo-ET) studies revealed unprecedented details of the interactions between stator unit and rotor. In this review, we summarize recent advances in our understanding of the structure and function of the flagellar stator unit, torque generation, and directional switching of the motor.",
author = "Haidai Hu and M{\`o}nica Santiveri and Navish Wadhwa and Berg, {Howard C} and Marc Erhardt and Taylor, {Nicholas M.I.}",
note = "Copyright {\textcopyright} 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.",
year = "2022",
doi = "10.1016/j.tibs.2021.06.005",
language = "English",
volume = "47",
pages = "160--172",
journal = "Trends in Biochemical Sciences",
issn = "0968-0004",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Structural basis of torque generation in the bi-directional bacterial flagellar motor

AU - Hu, Haidai

AU - Santiveri, Mònica

AU - Wadhwa, Navish

AU - Berg, Howard C

AU - Erhardt, Marc

AU - Taylor, Nicholas M.I.

N1 - Copyright © 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.

PY - 2022

Y1 - 2022

N2 - The flagellar stator unit is an oligomeric complex of two membrane proteins (MotA5B2) that powers bi-directional rotation of the bacterial flagellum. Harnessing the ion motive force across the cytoplasmic membrane, the stator unit operates as a miniature rotary motor itself to provide torque for rotation of the flagellum. Recent cryo-electron microscopic (cryo-EM) structures of the stator unit provided novel insights into its assembly, function, and subunit stoichiometry, revealing the ion flux pathway and the torque generation mechanism. Furthermore, in situ cryo-electron tomography (cryo-ET) studies revealed unprecedented details of the interactions between stator unit and rotor. In this review, we summarize recent advances in our understanding of the structure and function of the flagellar stator unit, torque generation, and directional switching of the motor.

AB - The flagellar stator unit is an oligomeric complex of two membrane proteins (MotA5B2) that powers bi-directional rotation of the bacterial flagellum. Harnessing the ion motive force across the cytoplasmic membrane, the stator unit operates as a miniature rotary motor itself to provide torque for rotation of the flagellum. Recent cryo-electron microscopic (cryo-EM) structures of the stator unit provided novel insights into its assembly, function, and subunit stoichiometry, revealing the ion flux pathway and the torque generation mechanism. Furthermore, in situ cryo-electron tomography (cryo-ET) studies revealed unprecedented details of the interactions between stator unit and rotor. In this review, we summarize recent advances in our understanding of the structure and function of the flagellar stator unit, torque generation, and directional switching of the motor.

U2 - 10.1016/j.tibs.2021.06.005

DO - 10.1016/j.tibs.2021.06.005

M3 - Review

C2 - 34294545

VL - 47

SP - 160

EP - 172

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 2

ER -

ID: 276699329