Switch I closure simultaneously promotes strong binding to actin and ADP in smooth muscle myosin.

ABSTRACT: The motor protein myosin uses energy derived from ATP hydrolysis to produce force and motion. Important conserved components (P-loop, switch I, and switch II) help propagate small conformational changes at the active site into large scale conformational changes in distal regions of the protein. Structural and biochemical studies have indicated that switch I may be directly responsible for the reciprocal opening and closing of the actin and nucleotide-binding pockets during the ATPase cycle, thereby aiding in the coordination of these important substrate-binding sites. Smooth muscle myosin has displayed the ability to simultaneously bind tightly to both actin and ADP, although it is unclear how both substrate-binding clefts could be closed if they are rigidly coupled to switch I. Here we us

SUBMITTER: Decarreau JA 

PROVIDER: S-EPMC3121376 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature