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Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2
Structural highlights
FunctionMYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Publication Abstract from PubMedThe 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. Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V.,Preller M, Bauer S, Adamek N, Fujita-Becker S, Fedorov R, Geeves MA, Manstein DJ J Biol Chem. 2011 Oct 7;286(40):35051-60. Epub 2011 Aug 13. PMID:21841195[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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