Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation.

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

SUBMITTER: Chang YW 

PROVIDER: S-EPMC3258884 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature