The 70-kDa heat-shock protein 70 (Hsp70) molecular chaperones have a nucleotide binding domain and a substrate binding domain that become allosterically coupled when Hsp70s bind ATP. The crystal structure of the prototypical Hsp70, Escherichia coli DnaK, in an ATP-bound state is now presented. The structure and functional analyses reveal the conformational changes and interdomain interactions that underlie allosteric coupling.
- Ruifeng Qi
- Evans Boateng Sarbeng
- Qinglian Liu
