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-Structure paper
Title | Molecular mechanism for rotational switching of the bacterial flagellar motor. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 27, Issue 11, Page 1041-1047, Year 2020 |
Publish date | Sep 7, 2020 |
![]() | Yunjie Chang / Kai Zhang / Brittany L Carroll / Xiaowei Zhao / Nyles W Charon / Steven J Norris / Md A Motaleb / Chunhao Li / Jun Liu / ![]() |
PubMed 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 ...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. |
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Methods | EM (subtomogram averaging) |
Resolution | 18.0 - 19.0 Å |
Structure data | ![]() EMDB-21884: ![]() EMDB-21885: ![]() EMDB-21886: |
Source |
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