Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.

@article{Mo2012SolutionSO,
  title={Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.},
  author={Guoya Mo and Hongjun Zhou and Tetsuya Kawamura and Frederick W. Dahlquist},
  journal={Biochemistry},
  year={2012},
  volume={51 18},
  pages={
          3786-98
        }
}
In the bacterial chemotaxis two-component signaling system, the histidine-containing phosphotransfer domain (the "P1" domain) of CheA receives a phosphoryl group from the catalytic domain (P4) of CheA and transfers it to the cognate response regulator (RR) CheY, which is docked by the P2 domain of CheA. Phosphorylated CheY then diffuses into the cytoplasm and interacts with the FliM moiety of the flagellar motors, thereby modulating the direction of flagellar rotation. Structures of various… CONTINUE READING
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