ArticleBiophysical journal2012
Three distinct actin-attached structural states of myosin in muscle fibers.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- Actin-binding compounds, previously discovered by FRET-based high-throughput screening, differentially affect skeletal and cardiac muscle.The Journal of biological chemistry · 2020Article
- Myosin and Other Energy-Transducing ATPases: Structural Dynamics Studied by Electron Paramagnetic Resonance.International journal of molecular sciences · 2020Review
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The myosin super-relaxed state is disrupted by estradiol deficiency.Biochemical and biophysical research communications · 2015Article
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.The Journal of biological chemistry · 2013Article
- Allosteric communication in Dictyostelium myosin II.Journal of muscle research and cell motility · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
We have used thiol cross-linking and electron paramagnetic resonance (EPR) to resolve structural transitions of myosin's light chain domain (LCD) and catalytic domain (CD) that are associated with force generation. Spin labels were incorporated into the LCD of muscle fibers by exchanging spin-labeled regulatory light chain for endogenous regulatory light chain, with full retention of function. To trap myosin in a structural state analogous to the elusive posthydrolysis ternary complex A.M'.D.P, we used pPDM to cross-link SH1 (Cys(707)) to SH2 (Cys(697)) on the CD. LCD orientation and dynamics were measured in three biochemical states: relaxation (A.M.T), SH1-SH2 cross-linked (A.M'.D.P analog), and rigor (A.M.D). EPR showed that the LCD of cross-linked fibers has an orientational distribution intermediate between relaxation and rigor, and saturation transfer EPR revealed slow rotational dynamics indistinguishable from that of rigor. Similar results were obtained for the CD using a bifunctional spin label to cross-link SH1-SH2, but the CD was more disordered than the LCD. We conclude that SH1-SH2 cross-linking traps a state in which both the CD and LCD are intermediate between relaxation (highly disordered and microsecond dynamics) and rigor (highly ordered and rigid), supporting the hypothesis that the cross-linked state is an A.M'D.P analog on the force generation pathway.
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Registered trials
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