Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants.

@article{Buczynski2001CharacterizationOA,
  title={Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants.},
  author={Greg Buczynski and Sergey V. Slepenkov and Michael G. Sehorn and Stephan N Witt},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 29},
  pages={27231-6}
}
The C-terminal, polypeptide binding domain of the 70-kDa molecular chaperone DnaK is composed of a unique lidlike subdomain that appears to hinder steric access to the peptide binding site. We have expressed, purified, and characterized a lidless form of DnaK to test the influence of the lid on the ATPase activity, on interdomain communication, and on the kinetics of peptide binding. The principal findings are that loss of the lid creates an activated form of DnaK which is not equivalent to ATP… CONTINUE READING