Abstract
Myosins are molecular motor proteins that harness the chemical energy stored in ATP to produce directed force along actin filaments. Complex communication pathways link the catalytic nucleotide-binding region, the structures responsible for force amplification and the actin-binding domain of myosin. We have crystallized the nucleotide-free motor domain of myosin II in a new conformation in which switch I and switch II, conserved loop structures involved in nucleotide binding, have moved away from the nucleotide-binding pocket. These movements are linked to rearrangements of the actin-binding region, which illuminate a previously unobserved communication pathway between the nucleotide-binding pocket and the actin-binding region, explain the reciprocal relationship between actin and nucleotide affinity and suggest a new mechanism for product release in myosin family motors.
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Acknowledgements
We thank W. Kabsch for crystallographic advice, S. Zimmermann and A. Scherer for excellent technical assistance, S. Fujita-Becker for in vitro motility analysis and K.C. Holmes for helpful comments, discussions and continuous support. The work was supported by Molecular Motors project grants from the Deutsche Forschungsgemeinschaft.
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Reubold, T., Eschenburg, S., Becker, A. et al. A structural model for actin-induced nucleotide release in myosin. Nat Struct Mol Biol 10, 826–830 (2003). https://doi.org/10.1038/nsb987
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DOI: https://doi.org/10.1038/nsb987
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