title: Review: The ATPase mechanism of myosin and actomyosin.
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. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 483-491, 2016.
authors.affiliation: School of Biosciences, University of Kent, Canterbury, UK.
authors.forename: Michael A
authors.initials: MA
authors.lastname: Geeves
mesh_terms: D000205:Actomyosin / Q000737:chemistry* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D006801:Humans; D006868:Hydrolysis; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins
keywords: ATPase mechanism; molecular motor; transition states