Abstract
The determination of the atomic structure of g-actin (Kabsch et al., 1990, see Fig. 1) allowed the development of an atomic model for f-actin (Holmes et al., 1990). The structure of f-actin was deduced from x-ray diffraction patterns from bundles of aligned actin filaments, using the known helical symmetry of the filament and keeping the atomic structure of the monomer fixed. The model of f-actin was obtained, therefore, using only four structural parameters: three rotational and one radial degree of freedom. The solution thus obtained is unique, and achieved an R-factor of.22; an extremely good fit with such few parameters.
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References
ben-Avraham, D., 1993, Vibrational normal-mode spectrum of globular proteins, Phys. Rev. B 47: 14559.
Brooks, B & Karplus, B., 1983, Harmonic dynamics of proteins: Normal modes and fluctuations in bovine pancreatic trypsin inhibitor, Biophysics 80: 6571.
Diamond, R., 1990, On the use of normal modes in thermal parameter refinement: theory and application to bovine pancreatic trypsin inhibitor, Acta Cryst. A46: 425.
Egelman E. H., Francis, N. & DeRosier, D. J., 1982, F-actin is a helix with a random variable twist, Nature 298: 131.
Flaherty K. M., McKay, D., Kabsch, W., & Holmes, K. C., 1991, Three-dimensional structure of the ATPase fragment of a 70kD heat-shock cognate protein, Proc. Natl. Acad. Sci. USA 88: 5041.
Goldstein, H., 1950, “Classical Mechanics”, Addison-Wesley, Reading, Massachusetts.
Hegyi G., Michel H., Shabanowitz J., Hunt D. F., Chatterjee N., Healy-Louie, G. and Elzinga, M., 1992, Gln-41 is intermolecularly cross-linked to lys-113 in f-actin by N-(4-azidobenzoyl)-putresine. Protein Science, 1: 132.
Holmes, K. C., Popp, D., Gebhard, W., Kabsch, W., 1990, Atomic model of the actin filament, Nature 347: 44.
Kabsch, W., Mannherz H. G., Suck, D., Pai, E., Holmes, K. C., 1990, Atomic structure of the actin: DNase I complex, Nature 347: 37.
Levitt, M., 1983, Molecular dynamics of native protein. I. Computer simulation of trajectories, J. Mol. Biol. 168: 595.
Levitt M., Sander, C. and Stern, P. S., 1985, Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme, J. Mol. Biol. 181: 423.
Millonig, R., Siitterlin, R., Engel, A., Pollard, T. D., Aebi, U., 1989, The ‘lateral slipping’ model of F-actin filaments, in: “Springer Series In Biophysics Vol. 3, Cytoskeletal and Extracellular Proteins” U. Aebi and A. Engel, eds., Springer-Verlag, Heidelberg
Orlova, A. and Egelman, E. H., 1993, A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. In press.
Steitz T. A., Anderson, W. F., Fletterick, R. J. & Anderson, C. M., 1977, High resolution crystal structures of yeasts hexokinase complexes with substrates, activators, and inhibitors. Evidence of an allosteric control site, J. Biol.Chem. 252: 4494.
Tirion M. M., & ben-Avraham, D., 1993, Normal mode analysis of g-actin, J. Mol. Biol. 230: 186.
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Tirion, M.M., ben-Avraham, D., Holmes, K.C. (1994). Vibrational Modes of G-Actin. In: Estes, J.E., Higgins, P.J. (eds) Actin. Advances in Experimental Medicine and Biology, vol 358. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2578-3_1
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