Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 27, Issue 11, Pages 1041-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41594-020-0497-2
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Funding
- National Institute of Allergy and Infectious Diseases [R01AI087946, R01AI078958, R01AI132818, R01AI59048]
- National Institute of Dental and Craniofacial Research [R01DE023080]
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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 useBorrelia burgdorferias 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.
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