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

1993; American Association for the Advancement of Science; Volume: 261; Issue: 5117 Linguagem: Inglês

10.1126/science.8316857

1095-9203

Ivan Rayment, W. Rypniewski, Karen Schmidt‐Bäse, Robert W. Smith, D.R. Tomchick, Matthew M. Benning, Donald A. Winkelmann, G.E. Wesenberg, Hazel M. Holden,

Muscle Physiology and Disorders

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.