The bacterial flagellar cap as the rotary promoter of flagellin self-assembly

K. Yonekura, S. Maki, D. G. Morgan, D. J. DeRosier, F. Vonderviszt, K. Imada, K. Namba

Research output: Contribution to journalArticlepeer-review

154 Citations (Scopus)

Abstract

The growth of the bacterial flagellar filament occurs at its distal end by self-assembly of flagellin transported from the cytoplasm through the narrow central channel. The cap at the growing end is essential for its growth, remaining stably attached while permitting the flagellin insertion. In order to understand the assembly mechanism, we used electron microscopy to study the structures of the cap-filament complex and isolated cap dimer. Five leg-like anchor domains of the pentameric cap flexibly adjusted their conformations to keep just one flagellin binding site open, indicating a cap rotation mechanism to promote the flagellin self-assembly. This represents one of the most dynamic movements in protein structures.

Original languageEnglish
Pages (from-to)2148-2152
Number of pages5
JournalScience
Volume290
Issue number5499
DOIs
Publication statusPublished - 2000 Dec 15
Externally publishedYes

ASJC Scopus subject areas

  • General

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