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Science 2 July 1993:
Vol. 261. no. 5117, pp. 50 - 58
DOI: 10.1126/science.8316857

Articles

Science, Vol 261, Issue 5117, 50-58
Copyright © 1993 by American Association for the Advancement of Science


articles

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

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

Department of Biochemistry, University of Wisconsin, Madison 53705.

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.


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Br. J. Anaesth. 90, 759-765
   Abstract »    Full Text »    PDF »
She4p/Dim1p Interacts with the Motor Domain of Unconventional Myosins in the Budding Yeast, Saccharomyces cerevisiae.
H. Toi, K. Fujimura-Kamada, K. Irie, Y. Takai, S. Todo, and K. Tanaka (2003)
Mol. Biol. Cell 14, 2237-2249
   Abstract »    Full Text »    PDF »
Suppression of Muscle Hypercontraction by Mutations in the Myosin Heavy Chain Gene of Drosophila melanogaster.
U. Nongthomba, M. Cummins, S. Clark, J. O. Vigoreaux, and J. C. Sparrow (2003)
Genetics 164, 209-222
   Abstract »    Full Text »    PDF »
Different degrees of lever arm rotation control myosin step size.
D. Kohler, C. Ruff, E. Meyhofer, and M. Bahler (2003)
J. Cell Biol. 161, 237-241
   Abstract »    Full Text »    PDF »
The converter domain modulates kinetic properties of Drosophila myosin.
K. P. Littlefield, D. M. Swank, B. M. Sanchez, A. F. Knowles, D. M. Warshaw, and S. I. Bernstein (2003)
Am J Physiol Cell Physiol 284, C1031-C1038
   Abstract »    Full Text »    PDF »
Myosin isoforms show unique conformations in the actin-bound state.
N. Volkmann, G. Ouyang, K. M. Trybus, D. J. DeRosier, S. Lowey, and D. Hanein (2003)
PNAS 100, 3227-3232
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Solution Structure of Heavy Meromyosin by Small-angle Scattering.
S. P. Harris, W. T. Heller, M. L. Greaser, R. L. Moss, and J. Trewhella (2003)
J. Biol. Chem. 278, 6034-6040
   Abstract »    Full Text »    PDF »
The prepower stroke conformation of myosin V.
S. Burgess, M. Walker, F. Wang, J. R. Sellers, H. D. White, P. J. Knight, and J. Trinick (2002)
J. Cell Biol. 159, 983-991
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Early stages of energy transduction by myosin: Roles of Arg in Switch I, of Glu in Switch II, and of the salt-bridge between them.
H. Onishi, T. Ohki, N. Mochizuki, and M. F. Morales (2002)
PNAS 99, 15339-15344
   Abstract »    Full Text »    PDF »
Maternal dexamethasone treatment alters myosin isoform expression and contractile dynamics in fetal arteries.
C.-M. Hai, G. Sadowska, L. Francois, and B. S. Stonestreet (2002)
Am J Physiol Heart Circ Physiol 283, H1743-H1749
   Abstract »    Full Text »    PDF »



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