Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.

@article{Drake1993ActivationOT,
  title={Activation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineering.},
  author={Steven K. Drake and Robert B. Bourret and Linda A. Luck and Melvin I. Simon and Joseph J. Falke},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 18},
  pages={13081-8}
}
CheY, the 14-kDa response regulator protein of the Escherichia coli chemotaxis pathway, is activated by phosphorylation of Asp57. In order to probe the structural changes associated with activation, an approach which combines 19F NMR, protein engineering, and the known crystal structure of one conformer has been utilized. This first of two papers examines the effects of Mg(II) binding and phosphorylation on the conformation of CheY. The molecule was selectively labeled at its six phenylalanine… CONTINUE READING