2V7Z

Crystal structure of the 70-kDa heat shock cognate protein from Rattus norvegicus in post-ATP hydrolysis state

Summary for 2V7Z

• Entry DOI: 10.2210/pdb2v7z/pdb
• Descriptor: HEAT SHOCK COGNATE 71 KDA PROTEIN, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: domain rearrangement, hsp70, hsc70, atpase, nucleus, chaperone, cytoplasm, nucleotide-binding, heat shock protein, atp-binding, phosphorylation, stress response
• Biological source: RATTUS NORVEGICUS
• Cellular location: Cytoplasm (By similarity): Q4FZY7
• Total number of polymer chains: 2
• Total formula weight: 120835.46

Authors

Chang, Y.-W.,Sun, Y.-J.,Wang, C.,Hsiao, C.-D. (deposition date: 2007-08-02, release date: 2008-04-08, Last modification date: 2023-12-13)

Primary citation

Chang, Y.-W.,Sun, Y.-J.,Wang, C.,Hsiao, C.-D.
Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation.
J.Biol.Chem., 283:15502-, 2008

PubMed Abstract: The 70-kDa heat shock proteins (Hsp70s) are highly conserved ATP-dependent molecular chaperones composed of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD) in a bilobate structure. Interdomain communication and nucleotide-dependent structural motions are critical for Hsp70 chaperone functions. Our understanding of these functions remains elusive due to insufficient structural information on intact Hsp70s that represent the different states of the chaperone cycle. We report here the crystal structures of DnaK from Geobacillus kaustophilus HTA426 bound with ADP-Mg(2+)-P(i) at 2.37A and the 70-kDa heat shock cognate protein from Rattus norvegicus bound with ADP-P(i) at 3.5A(.) The NBD and SBD in these structures are significantly separated from each other, and they might depict the ADP-bound conformation. Moreover, a Trp reporter was introduced at the potential interface region between NBD and the interdomain linker of GkDnaK to probe environmental changes. Results from fluorescence measurements support the notion that substrate binding enhances the domain-disjoining behavior of Hsp70 chaperones.

PubMed: 18400763
DOI: 10.1074/JBC.M708992200

Experimental method

X-RAY DIFFRACTION (3.5 Å)