Abstract
ELUCIDATION of the molecular contacts between actin and myosin is central to understanding the force-generating process in muscle and other cells. Actin, a highly conserved globular protein found in all eukaryotes, polymerizes into filaments (F-actin) for most of its biological functions. Myosins, which are more diverse in sequence, share a conserved globular head of about 900 amino acids in length (subfragment-1 or S1) at the N-terminal end of the molecule. S1 contains all the elements necessary for mechano-chemical force transduction in vitro1,2. Here we report an atomic model for the actomyosin complex produced by combining the atomic X-ray structure of F-actin3,4 and chicken myosin S15 with a three-dimensional reconstruction from electron micrographs of frozen-hydrated F-actin decorated with recombinant Dictyostelium myosin S1. The accuracy of the reconstruction shows the position of actin and myosin molecules unambiguously.
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Schröder, R., Manstein, D., Jahn, W. et al. Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature 364, 171–174 (1993). https://doi.org/10.1038/364171a0
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DOI: https://doi.org/10.1038/364171a0
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