Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V.

Preller, Matthias and Bauer, Stefanie and Adamek, N. and Fujita-Becker, Setsuko and Fedorov, Roman and Geeves, M.A. and Manstein, Dietmar J (2011) Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V. The Journal of biological chemistry, 286 (40). pp. 35051-35060. ISSN 1083-351X.

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Official URL
http://dx.doi.org/10.1074/jbc.M111.265298

Abstract

The cold-sensitive single-residue mutation of glycine 680 in the reactive thiol region of Dictyostelium discoideum myosin-2 or the corresponding conserved glycine in other myosin isoforms has been reported to interfere with motor function. Here we present the x-ray structures of myosin motor domain mutants G680A in the absence and presence of nucleotide as well as the apo structure of mutant G680V. Our results show that the Gly-680 mutations lead to uncoupling of the reactive thiol region from the surrounding structural elements. Structural and functional data indicate that the mutations induce the preferential population of a state that resembles the ADP-bound state. Moreover, the Gly-680 mutants display greatly reduced dynamic properties, which appear to be related to the recovery of myosin motor function at elevated temperatures.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 03 Nov 2011 12:19
Last Modified: 17 Apr 2012 13:19
Resource URI: http://kar.kent.ac.uk/id/eprint/28345 (The current URI for this page, for reference purposes)
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