Flagellar movement driven by proton translocation.
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.
Blair
David F
DF
Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, UT 84112-0840, USA. blair@bioscience.utah.edu
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D005407:Flagella / Q000502:physiology* / Q000648:ultrastructure; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D017136:Ion Transport; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D009068:Movement; D009154:Mutation; D011522:Protons
D001426:Bacterial Proteins; D007473:Ion Channels; D020409:Molecular Motor Proteins; D011522:Protons