Electron cryomicroscopic visualization of PomA/B stator units of the sodium-driven flagellar motor in liposomes

Koji Yonekura, Toshiharu Yakushi, Tatsuo Atsumi, Saori Maki-Yonekura, Michio Homma, Keiichi Namba

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

A motor protein complex of the bacterial flagellum, PomA/B from Vibrio alginolyticus, was reconstituted into liposomes and visualized by electron cryomicroscopy. PomA/B is a sodium channel, composed of two membrane proteins, PomA and PomB, and converts ion flux to the rotation of the flagellar motor. Escherichia coli and Salmonella have a homolog called MotA/B, which utilizes proton instead of sodium ion. PomB and MotB have a peptidoglycan-binding motif in their C-terminal region, and therefore PomA/B and MotA/B are regarded as the stator. Energy filtering electron cryomicroscopy enhanced the image contrast of the proteins reconstituted into liposomes and showed that two extramembrane domains with clearly different sizes stick out of the lipid bilayers on opposite sides. Image analysis combined with gold labeling and deletion of the peptidoglycan-binding motif revealed that the longer one, ∼70 Å long, is likely to correspond to the periplasmic domain, and the other, about half size, to the cytoplasmic domain.

Original languageEnglish
Pages (from-to)73-81
Number of pages9
JournalJournal of Molecular Biology
Volume357
Issue number1
DOIs
Publication statusPublished - 2006 Mar 17
Externally publishedYes

Keywords

  • Bacterial flagellum
  • Energy filtering electron cryomicroscopy
  • Flagellar motor
  • Liposome
  • Stator

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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