DOI: 10.1073/pnas.96.18.10134. Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor

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

10.1073/pnas.96.18.10134

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

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.

Bibliography

Thomas, D. R., Morgan, D. G., & DeRosier, D. J. (1999). Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor. Proceedings of the National Academy of Sciences, 96(18), 10134â10139.

Authors 3

Dennis R. Thomas (first)
David Gene Morgan (additional)
David J. DeRosier (additional)

References 37 Referenced 132

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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 10:38 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 4:33 p.m.)
Indexed	5 months, 1 week ago (March 19, 2025, 12:19 p.m.)
Issued	25 years, 11 months ago (Aug. 31, 1999)
Published	25 years, 11 months ago (Aug. 31, 1999)
Published Online	25 years, 11 months ago (Aug. 31, 1999)
Published Print	25 years, 11 months ago (Aug. 31, 1999)

Funders 0

None

BibTeX

@article{Thomas_1999, title={Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.18.10134}, DOI={10.1073/pnas.96.18.10134}, number={18}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Thomas, Dennis R. and Morgan, David Gene and DeRosier, David J.}, year={1999}, month=aug, pages={10134–10139} }

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  "abstract": "<jats:p>FliG, FliM, and FliN, key proteins for torque generation, are\n located in two rings. The first protein is in the M ring and the last\n two are in the C ring. The rotational symmetries of the C and M rings\n have been determined to be about 34 (this paper) and 26 (previous\n work), respectively. The mechanism proposed here depends on the\n symmetry mismatch between the rings: the C ring extends 34 levers, of\n which 26 can bind to the 26 equivalent sites on the M ring. The\n remaining 8 levers bind to proton\u2013pore complexes (studs) to form 8\n torque generators. Movement results from the swapping of stud-bound\n levers with M ring-bound levers. The model predicts that both the M and\n C rings rotate in the same direction but at different speeds.</jats:p>",
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