Three-dimensional structure of myosin subfragment-1: a molecular motor.
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.
Rayment
I
I
Department of Biochemistry, University of Wisconsin, Madison 53705.
Rypniewski
W R
WR
Schmidt-Bäse
K
K
Smith
R
R
Tomchick
D R
DR
Benning
M M
MM
Winkelmann
D A
DA
Wesenberg
G
G
Holden
H M
HM
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
D000199:Actins; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate