Article
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones.
Cell - 7 Dec 2012
Zhuravleva Anastasia, Clerico Eugenia M, Gierasch Lila M
Abstract excerpt
The allosteric mechanism of Hsp70 molecular chaperones enables ATP binding to the N-terminal nucleotide-binding domain (NBD) to alter substrate affinity to the C-terminal substrate-binding domain (SBD) and substrate binding to enhance ATP hydrolysis. Cycling between ATP-bound and ADP/substrate-bound states requires Hsp70s to visit a state with high ATPase activity and fast on/off kinetics of substrate binding. We...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.