title: Three-dimensional structure of myosin subfragment-1: a molecular motor.
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.
authors.affiliation: Department of Biochemistry, University of Wisconsin, Madison 53705.
authors.forename: I
authors.initials: I
authors.lastname: Rayment
authors.forename: W R
authors.initials: WR
authors.lastname: Rypniewski
authors.forename: K
authors.initials: K
authors.lastname: Schmidt-Bäse
authors.forename: R
authors.initials: R
authors.lastname: Smith
authors.forename: D R
authors.initials: DR
authors.lastname: Tomchick
authors.forename: M M
authors.initials: MM
authors.lastname: Benning
authors.forename: D A
authors.initials: DA
authors.lastname: Winkelmann
authors.forename: G
authors.initials: G
authors.lastname: Wesenberg
authors.forename: H M
authors.initials: HM
authors.lastname: Holden
mesh_terms: D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D007091:Image Processing, Computer-Assisted; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009119:Muscle Contraction; D015879:Myosin Subfragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate