Ontology highlight
ABSTRACT:
SUBMITTER: Swain JF
PROVIDER: S-EPMC1894942 | biostudies-literature | 2007 Apr
REPOSITORIES: biostudies-literature
Swain Joanna F JF Dinler Gizem G Sivendran Renuka R Montgomery Diana L DL Stotz Mathias M Gierasch Lila M LM
Molecular cell 20070401 1
Hsp70 chaperones assist in protein folding, disaggregation, and membrane translocation by binding to substrate proteins with an ATP-regulated affinity that relies on allosteric coupling between ATP-binding and substrate-binding domains. We have studied single- and two-domain versions of the E. coli Hsp70, DnaK, to explore the mechanism of interdomain communication. We show that the interdomain linker controls ATPase activity by binding to a hydrophobic cleft between subdomains IA and IIA. Furthe ...[more]