ArticleNature communications2017
Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 87 citations in OpenAlex.
- The structure of the native cardiac crossbridge in the rigor state.Science advances · 2026Article
- Elucidating chiral myosin-induced actin dynamics: From single-filament behavior to collective structures.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Human cardiac β-myosin powerstroke energetics: Thin filament, Pi displacement, and mutation effects.Biophysical journal · 2024Article
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- GRespiratory research · 2024Review
- Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.Molecules (Basel, Switzerland) · 2024Article
- Myosin's powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin.The Journal of general physiology · 2024Article
- Sequence Alignment-Based Prediction of Myosin 7A: Structural Implications and Protein Interactions.International journal of molecular sciences · 2024Article
- Article
- Are the class 18 myosins Myo18A and Myo18B specialist sarcomeric proteins?Frontiers in physiology · 2024Review
- From amino-acid to disease: the effects of oxidation on actin-myosin interactions in muscle.Journal of muscle research and cell motility · 2023Review
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- Integrating comparative modeling and accelerated simulations reveals conformational and energetic basis of actomyosin force generation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Divergent Plasmodium actin residues are essential for filament localization, mosquito salivary gland invasion and malaria transmission.PLoS pathogens · 2022Article
- High-resolution structures of malaria parasite actomyosin and actin filaments.PLoS pathogens · 2022Article
- The R369 Myosin Residue within Loop 4 Is Critical for Actin Binding and Muscle Function inInternational journal of molecular sciences · 2022Article
- Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Thin filament cardiomyopathies: A review of genetics, disease mechanisms, and emerging therapeutics.Frontiers in cardiovascular medicine · 2022Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because of the absence of actomyosin rigour structure at high resolution, it still remains unclear how the strong binding of myosin to actin filament triggers the release of hydrolysis products and how ATP binding causes their dissociation. Here we report the structure of mammalian skeletal muscle actomyosin rigour complex at 5.2 Å resolution by electron cryomicroscopy. Comparison with the structures of myosin in various states shows a distinctly large conformational change, providing insights into the ATPase-coupled reaction cycle of actomyosin. Based on our observations, we hypothesize that asymmetric binding along the actin filament could function as a Brownian ratchet by favouring directionally biased thermal motions of myosin and actin.
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