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PMID: 8316857 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Science (New York, N.Y.) ·Vol. 261 ·No. 5117 ·1993-07-02 ·Pages 50-8

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

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 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.

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,metabolism Protein Conformation Protein Structure, Secondary X-Ray Diffraction
Chemicals
Actins Myosin Subfragments Adenosine Triphosphate
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Rayment I
Department of Biochemistry, University of Wisconsin, Madison 53705.
Rypniewski W R
Schmidt-Bäse K
Smith R
Tomchick D R
Benning M M
Winkelmann D A
Wesenberg G
Holden H M
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1993-07-02
Pages
50-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Corrections
CommentIn
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