Conformational change of flagellin for polymorphic supercoiling of the flagellar filament

Saori Maki-Yonekura, Koji Yonekura, Keiichi Namba

Research output: Contribution to journalArticlepeer-review

73 Citations (Scopus)

Abstract

The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left-and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.

Original languageEnglish
Pages (from-to)417-422
Number of pages6
JournalNature Structural and Molecular Biology
Volume17
Issue number4
DOIs
Publication statusPublished - 2010 Apr
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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