The ATPase mechanism of myosin and actomyosin

Geeves, Michael A. (2016) The ATPase mechanism of myosin and actomyosin. Biopolymers, 105 . pp. 483-491. ISSN 0006-3525. (doi:https://doi.org/10.1002/bip.22853) (Full text available)

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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. This article is protected by copyright. All rights reserved.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 06 May 2016 15:56 UTC
Last Modified: 01 Aug 2018 08:58 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/55320 (The current URI for this page, for reference purposes)
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