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FEBS Lett. 2003 Jun 12;545(1):86-95.

Flagellar movement driven by proton translocation.

Author information

1
Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112-0840, USA. blair@bioscience.utah.edu

Abstract

The bacterial flagellar motor couples ion flow to rotary motion at high speed and with apparently fixed stoichiometry. The functional properties of the motor are quite well understood, but its molecular mechanism remains unknown. Recent studies of motor physiology, coupled with mutational and biochemical studies of the components, put significant constraints on the mechanism. Rotation is probably driven by conformational changes in membrane-protein complexes that form the stator. These conformational changes occur as protons move on and off a critical Asp residue in the stator protein MotB, and the resulting forces are applied to the rotor protein FliG.

PMID:
12788496
DOI:
10.1016/s0014-5793(03)00397-1
[Indexed for MEDLINE]
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