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

Trends Biochem Sci. 2022 Feb;47(2):160-172. doi: 10.1016/j.tibs.2021.06.005. Epub 2021 Jul 19.

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.

Keywords: bacterial flagellar motor; proton/sodium channel; stator unit; structural biology, cryo-electron microscopy; torque generation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / metabolism
  • Bacterial Proteins* / chemistry
  • Cryoelectron Microscopy / methods
  • Flagella* / chemistry
  • Flagella* / metabolism
  • Flagella* / ultrastructure
  • Torque

Substances

  • Bacterial Proteins