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Three-dimensional structure of myosin subfragment-1: a molecular motor
I Rayment1, W R Rypniewski, K Schmidt-Bäse
1Department of Biochemistry, University of Wisconsin, Madison 53705.
Science (New York, N.Y.)
|July 2, 1993
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.