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. (doi:https://doi.org/10.1074/jbc.M111.265298) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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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 > Sciences > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||03 Nov 2011 12:19 UTC|
|Last Modified:||14 Jul 2014 12:13 UTC|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/28345 (The current URI for this page, for reference purposes)|