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

Science. 1993 Jul 2;261(5117):50-8. doi: 10.1126/science.8316857.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Binding Sites
  • Crystallization
  • Image Processing, Computer-Assisted
  • Methylation
  • Models, Molecular*
  • Molecular Sequence Data
  • Muscle Contraction
  • Myosin Subfragments / chemistry*
  • Myosin Subfragments / metabolism
  • Protein Conformation*
  • Protein Structure, Secondary
  • X-Ray Diffraction


  • Actins
  • Myosin Subfragments
  • Adenosine Triphosphate