Structure of the flagellar motor protein complex pomAB: Implications for the torque-generating conformation

Koji Yonekura, Saori Maki-Yonekura, Michio Homma

研究成果: Article査読

38 被引用数 (Scopus)

抄録

The bacterial flagellar motor is driven by an ion flux through a channel called MotAB in Escherichia coli or Salmonella and PomAB in Vibrio alginolyticus. PomAB is composed of two transmembrane (TM) components, PomA and PomB, and converts a sodium ion flux to rotation of the flagellum. Its homolog, MotAB, utilizes protons instead of sodium ions. PomB/MotB has a peptidoglycan (PG)-binding motif in the periplasmic domain, allowing it to function as the stator by being anchored to the PG layer. To generate torque, PomAB/MotAB is thought to undergo a conformational change triggered by the ion flux and to interact directly with FliG, a component of the rotor. Here, we present the first three-dimensional structure of this torque-generating stator unit analyzed by electron microscopy. The structure of PomAB revealed two arm domains, which contain the PG-binding site, connected to a large base made of the TM and cytoplasmic domains. The arms lean downward to the membrane surface, likely representing a "plugged" conformation, which would prevent ions leaking through the channel. We propose a model for how PomAB units are placed around the flagellar basal body to function as torque generators.

本文言語English
ページ(範囲)3863-3870
ページ数8
ジャーナルJournal of bacteriology
193
15
DOI
出版ステータスPublished - 2011 8月
外部発表はい

ASJC Scopus subject areas

  • 微生物学
  • 分子生物学

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