| Literature DB >> 27061920 |
Abstract
Myosins are a large family of molecular motors that use the common P-loop, Switch 1 and Switch 2 nucleotide binding motifs to recognize ATP, to create a catalytic site than can efficiently hydrolyze ATP and to communicate the state of the nucleotide pocket to other allosteric binding sites on myosin. The energy of ATP hydrolysis is used to do work against an external load. In this short review I will outline current thinking on the mechanism of ATP hydrolysis and how the energy of ATP hydrolysis is coupled to a series of protein conformational changes that allow a myosin, with the cytoskeleton track actin, to operate as a molecular motor of distinct types; fast movers, processive motors or strain sensors.Entities:
Keywords: ATPase mechanism; molecular motor; transition states
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Year: 2016 PMID: 27061920 DOI: 10.1002/bip.22853
Source DB: PubMed Journal: Biopolymers ISSN: 0006-3525 Impact factor: 2.505