Publication Date:
1993-07-02
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rayment, I -- Rypniewski, W R -- Schmidt-Base, K -- Smith, R -- Tomchick, D R -- Benning, M M -- Winkelmann, D A -- Wesenberg, G -- Holden, H M -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):50-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Wisconsin, Madison 53705.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316857" target="_blank"〉PubMed〈/a〉
Keywords:
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
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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