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. 1993 Jul 2;261(5117):50-8.
doi: 10.1126/science.8316857.

Three-dimensional structure of myosin subfragment-1: a molecular motor

I Rayment  1 , W R Rypniewski, K Schmidt-Bäse, R Smith, D R Tomchick, M M Benning, D A Winkelmann, G Wesenberg, H M Holden
Affiliations

Three-dimensional structure of myosin subfragment-1: a molecular motor

I Rayment et al. Science. .

Abstract

Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

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Comment in

  • Molecular muscle.
    Taylor EW. Taylor EW. Science. 1993 Jul 2;261(5117):35-6. doi: 10.1126/science.8316856. Science. 1993. PMID: 8316856 No abstract available.

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