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Vol. 96, Issue 18, 10134-10139, August 31, 1999

Biophysics
 Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor

Dennis R. Thomas*, David Gene Morgandagger , and David J. DeRosierDagger

W. M. Keck Institute for Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, MA 02254

Communicated by Howard C. Berg, Harvard University, Cambridge, MA, June 11, 1999 (received for review April 3, 1999)

FliG, FliM, and FliN, key proteins for torque generation, are located in two rings. The first protein is in the M ring and the last two are in the C ring. The rotational symmetries of the C and M rings have been determined to be about 34 (this paper) and 26 (previous work), respectively. The mechanism proposed here depends on the symmetry mismatch between the rings: the C ring extends 34 levers, of which 26 can bind to the 26 equivalent sites on the M ring. The remaining 8 levers bind to proton-pore complexes (studs) to form 8 torque generators. Movement results from the swapping of stud-bound levers with M ring-bound levers. The model predicts that both the M and C rings rotate in the same direction but at different speeds.

*   Present address: Structural Biology Program, European Molecular Biology Laboratory, Heidelberg 69117, Germany.
dagger    Present address: The Department of Biophysics, Boston University School of Medicine, Boston, MA 02118 and Department of Cell Biology, Harvard Medical School, Boston, MA 02254.
Dagger    To whom reprint requests should be addressed.

Copyright © 1999 by The National Academy of Sciences  0027-8424/99/9610134-6$2.00/0
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