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Atomic model of the actin filament

MPS-Authors
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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;

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Gebhard,  Werner
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
IT Group / Data processing, Max Planck Institute for Medical Research, Max Planck Society;

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Kabsch,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Holmes, K. C., Popp, D., Gebhard, W., & Kabsch, W. (1990). Atomic model of the actin filament. Nature, 347, 44-49. doi:doi:10.1038/347044a0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AD17-3
Abstract
The F-actin filament has been constructed from the atomic structure of the actin monomer to fit the observed X-ray fibre diagram from oriented gels of F-actin. A unique orientation of the monomer with respect to the actin helix has been found. The main interactions are along the two-start helix with a contribution from a loop extending across the filament axis provided by the molecule in the adjacent strand. There are also contacts along the left-handed genetic helix.