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Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

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  • Takashi Fujii

    (Graduate School of Frontier Biosciences, Osaka University, and Riken Quantitative Biology Center)

  • Keiichi Namba

    (Graduate School of Frontier Biosciences, Osaka University, and Riken Quantitative Biology Center)

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.

Suggested Citation

  • Takashi Fujii & Keiichi Namba, 2017. "Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism," Nature Communications, Nature, vol. 8(1), pages 1-11, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms13969
    DOI: 10.1038/ncomms13969
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