ArticleThe Journal of biological chemistry2011
Structural basis for the allosteric interference of myosin function by reactive thiol region mutations G680A and G680V.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Switch-2 determines MgFrontiers in physiology · 2024Article
- Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations.Frontiers in molecular biosciences · 2021Article
- Unraveling a Force-Generating Allosteric Pathway of Actomyosin Communication Associated with ADP and PInternational journal of molecular sciences · 2020Article
- Full-lengtheLife · 2020Article
- Structural and Computational Insights into a Blebbistatin-Bound Myosin•ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.International journal of molecular sciences · 2020Article
- Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism.Nature communications · 2019Article
- Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- ADisease models & mechanisms · 2017Article
- Article
- Rational elicitation of cold-sensitive phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Patterns of database citation in articles and patents indicate long-term scientific and industry value of biological data resources.F1000Research · 2016Article
- Mammalian myosin-18A, a highly divergent myosin.The Journal of biological chemistry · 2013Article
- Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness.Molecular biology of the cell · 2012Article
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Authors and funding
7 authors.
Funding
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.
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