Report

The Bacterial Flagellar Cap as the Rotary Promoter of Flagellin Self-Assembly

Science  15 Dec 2000:
Vol. 290, Issue 5499, pp. 2148-2152
DOI: 10.1126/science.290.5499.2148

You are currently viewing the abstract.

View Full Text
As a service to the community, AAAS/Science has made this article free with registration.

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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: keiichi{at}crl.mei.co.jp

View Full Text

Cited By...