Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.

@article{Buchberger1995NucleotideinducedCC,
  title={Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication.},
  author={Alexander Buchberger and H Theyssen and Hartwig Schr{\"o}der and John S. McCarty and G Virgallita and Philipp Milkereit and Jochen Reinstein and Bernd Bukau},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 28},
  pages={
          16903-10
        }
}
Interactions of the DnaK (Hsp70) chaperone from Escherichia coli with substrates are controlled by ATP. Nucleotide-induced changes in DnaK conformation were investigated by monitoring changes in tryptic digestion pattern and tryptophan fluorescence. Using nucleotide-free DnaK preparations, not only the known ATP-induced major changes in kinetics and pattern of proteolysis but also minor ADP-induced changes were detected. Similar ATP-induced conformational changes occurred in the DnaK-T199A… CONTINUE READING
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