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Science 2 July 1993:
Vol. 261. no. 5117, pp. 50 - 58
DOI: 10.1126/science.8316857
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Articles

Science, Vol 261, Issue 5117, 50-58
Copyright © 1993 by American Association for the Advancement of Science

articles

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

I Rayment, WR Rypniewski, K Schmidt-Base, R Smith, DR Tomchick, MM Benning, DA Winkelmann, G Wesenberg, and HM Holden

Department of Biochemistry, University of Wisconsin, Madison 53705.

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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