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

Research output: Contribution to journalArticlepeer-review

1804 Scopus citations

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 - 1993

ASJC Scopus subject areas

  • General

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