ArticleProceedings of the National Academy of Sciences of the United States of America2003
Myosin isoforms show unique conformations in the actin-bound state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- The structure of the actin-smooth muscle myosin motor domain complex in the rigor state.Journal of structural biology · 2017Article
- Flexibility within the heads of muscle myosin-2 molecules.Journal of molecular biology · 2014Article
- Article
- G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.The Journal of biological chemistry · 2012Article
- Myosin binding surface on actin probed by hydroxyl radical footprinting and site-directed labels.Journal of molecular biology · 2011Article
- Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain.Journal of molecular biology · 2011Article
- Myosin isoform determines the conformational dynamics and cooperativity of actin filaments in the strongly bound actomyosin complex.Journal of molecular biology · 2010Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.Journal of molecular biology · 2008Article
- Functional effects of the hypertrophic cardiomyopathy R403Q mutation are different in an alpha- or beta-myosin heavy chain backbone.The Journal of biological chemistry · 2008Article
- The R403Q myosin mutation implicated in familial hypertrophic cardiomyopathy causes disorder at the actomyosin interface.PloS one · 2007Article
- Diversity of structural behavior in vertebrate conventional myosins complexed with actin.Journal of molecular biology · 2007Article
- A variable domain near the ATP-binding site in Drosophila muscle myosin is part of the communication pathway between the nucleotide and actin-binding sites.Journal of molecular biology · 2007Article
- Mechanochemical coupling in the myosin motor domain. II. Analysis of critical residues.PLoS computational biology · 2007Article
- Dynamics of the nucleotide pocket of myosin measured by spin-labeled nucleotides.Biophysical journal · 2007Article
- Cardiac myosin missense mutations cause dilated cardiomyopathy in mouse models and depress molecular motor function.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Structural rearrangements in the active site of smooth-muscle myosin.Biophysical journal · 2005Article
- The motor mechanism of myosin V: insights for muscle contraction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
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6 authors.
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Abstract
Crystallographic data for several myosin isoforms have provided evidence for at least two conformations in the absence of actin: a prehydrolysis state that is similar to the original nucleotide-free chicken skeletal subfragment-1 (S1) structure, and a transition-state structure that favors hydrolysis. These weak-binding states differ in the extent of closure of the cleft that divides the actin-binding region of the myosin and the position of the light chain binding domain or lever arm that is believed to be associated with force generation. Previously, we provided insights into the interaction of smooth-muscle S1 with actin by computer-based fitting of crystal structures into three-dimensional reconstructions obtained by electron cryomicroscopy. Here, we analyze the conformations of actin-bound chicken skeletal muscle S1. We conclude that both myosin isoforms in the nucleotide-free, actin-bound state can achieve a more tightly closed cleft, a more downward position of the lever arm, and more stable surface loops than those seen in the available crystal structures, indicating the existence of unique actin-bound conformations.
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