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Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1

MPG-Autoren
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Schröder,  Rasmus R.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Manstein,  Dietmar J.
Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Jahn,  Werner
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://www.nature.com/nature/journal/v364/n6433/pdf/364171a0.pdf
(beliebiger Volltext)

https://dx.doi.org/10.1038/364171a0
(beliebiger Volltext)

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Zitation

Schröder, R. R., Manstein, D. J., Jahn, W., Holden, H. M., Rayment, I., Holmes, K. C., et al. (1993). Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature, 364, 171-174. doi:10.1038/364171a0.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-AA2D-B
Zusammenfassung
ELUCIDATION of the molecular contacts between actin and myosin is central to understanding the force-generating process in muscle and other cells. Actin, a highly conserved globular protein found in all eukaryotes, polymerizes into filaments (F-actin) for most of its biological functions. Myosins, which are more diverse in sequence, share a conserved globular head of about 900 amino acids in length (subfragment-1 or S1) at the N-terminal end of the molecule. S1 contains all the elements necessary for mechano-chemical force transduction in vitro 1,2. Here we report an atomic model for the actomyosin complex produced by combining the atomic X-ray structure of F-actin3,4 and chicken myosin S15 with a three-dimensional reconstruction from electron micrographs of frozen-hydrated F-actin decorated with recombinant Dictyostelium myosin S1. The accuracy of the reconstruction shows the position of actin and myosin molecules unambiguously.