Helix rotation model of the flagellar rotary motor.
A new model of the flagellar motor is proposed that is based on established dynamics of the KcsA potassium ion channel and on known genetic, biochemical, and biophysical facts, which accounts for the mechanics of torque generation, force transmission, and reversals of motor rotation. It predicts that proton (or in some species sodium ion) flow generates short, reversible helix rotations of the MotA-MotB channel complex (the stator) that are transmitted by Coulomb forces to the FliG segments at the rotor surface. Channels are arranged as symmetric pairs, S and T, that swing back and forth in synchrony. S and T alternate in attaching to the rotor, so that force transmission proceeds in steps. The sense of motor rotation can be readily reversed by conformationally switching the position of charged groups on the rotor so that they interact with the stator during the reverse rather than forward strokes. An elastic device accounts for the observed smoothness of rotation and a prolonged attachment of the torque generators to the rotor, i.e., a high duty ratio of each torque-generating unit.
Schmitt
Rüdiger
R
Institute of Biochemistry, Genetics, and Microbiology, University of Regensburg, D-93040 Regensburg, Germany. rudy.schmitt@biologie.uni-regensburg.de
D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D003198:Computer Simulation; D005407:Flagella / Q000737:chemistry / Q000502:physiology*; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000502:physiology*; D015221:Potassium Channels / Q000737:chemistry / Q000502:physiology*; D012399:Rotation; D013314:Stress, Mechanical
D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; C063010:MotA protein, Bacteria; C064779:MotB protein, Bacteria; D015221:Potassium Channels; C107790:prokaryotic potassium channel