Molecular mechanism for rotational switching of the bacterial flagellar motor

Published Date
Journal
Nature Structural & Molecular Biology
Citation
Nat Struct Mol Biol 2020 Sep 7
DOI
10.1038/s41594-020-0497-2
Authors
Chang Y,
Zhang K
Carroll BL
Zhao X
Charon NW
Norris SJ
Motaleb MA
Li C
Liu J
Abstract

The bacterial flagellar motor can rotate in counterclockwise (CCW) or clockwise (CW) senses, and transitions are controlled by the phosphorylated form of the response regulator CheY (CheY-P). To dissect the mechanism underlying flagellar rotational switching, we use Borrelia burgdorferi as a model system to determine high-resolution in situ motor structures in cheX and cheY3 mutants, in which motors are locked in either CCW or CW rotation. The structures showed that CheY3-P interacts directly with a switch protein, FliM, inducing a major remodeling of another switch protein, FliG2, and altering its interaction with the torque generator. Our findings lead to a model in which the torque generator rotates in response to an inward flow of H+ driven by the proton motive force, and conformational changes in FliG2 driven by CheY3-P allow the switch complex to interact with opposite sides of the rotating torque generator, facilitating rotational switching.