Preller, Matthias and Bauer, Stefanie and Adamek, Nancy and Fujita-Becker, Setsuko and Fedorov, Roman and Geeves, Michael A. and Manstein, Dietmar J (2011) Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V. Journal Of Biological Chemistry, 286 (40). pp. 35051-35060. ISSN 0021-9258. (The full text of this publication is not available from this repository)
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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.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||03 Nov 2011 12:19|
|Last Modified:||15 Apr 2014 10:51|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/28345 (The current URI for this page, for reference purposes)|