Structure of the actin-myosin complex and its implications for muscle contraction

Science. 1993 Jul 2;261(5117):58-65. doi: 10.1126/science.8316858.


Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.

Publication types

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

MeSH terms

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


  • Actins
  • Myosin Subfragments
  • Adenosine Triphosphate
  • Actomyosin