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

Ivan Rayment, Wojciech R. Rypniewski, Karen Schmidt-Bäse, Robert Smith, Diana R. Tomchick, Matthew M. Benning, Donald A. Winkelmann, Gary Wesenberg, Hazel M. Holden

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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 acting 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.

Original languageEnglish (US)
Pages (from-to)50-58
Number of pages9
JournalScience
Volume261
Issue number5117
DOIs
StatePublished - Jan 1 1993

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Cite this

Rayment, I., Rypniewski, W. R., Schmidt-Bäse, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., & Holden, H. M. (1993). Three-dimensional structure of myosin subfragment-1: A molecular motor. Science, 261(5117), 50-58. https://doi.org/10.1126/science.8316857