Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching

Lawrence K. Lee, Michael A. Ginsburg, Claudia Crovace, Mhairi Donohoe and Daniela Stock ()
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Lawrence K. Lee: The Victor Chang Cardiac Research Institute, Lowy Packer Building, 405 Liverpool Street, Darlinghurst, New South Wales 2010, Australia
Michael A. Ginsburg: The Victor Chang Cardiac Research Institute, Lowy Packer Building, 405 Liverpool Street, Darlinghurst, New South Wales 2010, Australia
Claudia Crovace: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Mhairi Donohoe: The Victor Chang Cardiac Research Institute, Lowy Packer Building, 405 Liverpool Street, Darlinghurst, New South Wales 2010, Australia
Daniela Stock: The Victor Chang Cardiac Research Institute, Lowy Packer Building, 405 Liverpool Street, Darlinghurst, New South Wales 2010, Australia

Nature, 2010, vol. 466, issue 7309, 996-1000

Abstract: Ringing the direction changes Rotation of the bacterial flagellar filament is responsible for bacterial motility. The direction of rotation determines whether the bacteria run smoothly forward or tumble to change their trajectory. The flagellar motor drives this rotation either clockwise or counter-clockwise, with the direction regulated by the flagellar switch complex. One of its components, a ring-shaped protein called FliG, applies the twisting motion or torque that enables the motor to switch direction — a notable feat since the flagellum rotates at hundreds of revolutions per second, yet reverses direction in less than a millisecond. The full-length structure of FliG has now been determined, and the conformational changes that are involved in switching between the direction of rotation identified.

Date: 2010
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DOI: 10.1038/nature09300

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