Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima.

@article{Hamel2006ChemicalshiftperturbationMO,
  title={Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima.},
  author={Damon J. Hamel and Hongjun Zhou and Mary R. Starich and Richard Byrd and Frederick W. Dahlquist},
  journal={Biochemistry},
  year={2006},
  volume={45 31},
  pages={9509-17}
}
Regulating the activity of the histidine autokinase CheA is a central step in bacterial chemotaxis. The CheA autophosphorylation reaction minimally involves two CheA domains, denoted P1 and P4. The kinase domain (P4) binds adenosine triphosphate (ATP) and orients the gamma phosphate for phosphotransfer to a reactive histidine on the phosphoacceptor domain (P1). Three-dimensional triple-resonance experiments allowed sequential assignments of backbone nuclei from P1 and P4 domains as well as the… CONTINUE READING