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Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons93650

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;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94211

Mannherz,  Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Suck, D., Kabsch, W., & Mannherz, H. G. (1981). Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution. Proceedings of the National Academy of Sciences of the United States of America, 78(7), 4319-4323. doi:10.1073/pnas.78.7.4319.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0019-B073-1
Zusammenfassung
The structure of rabbit skeletal muscle actin complexed with bovine pancreatic DNase I has been determined by x-ray crystallographic methods at 6-A resolution. The analysis was based on a new orthorhombic crystal form, space group P212121, with one complex in the asymmetric unit. Six isomorphous heavy-atom derivatives yielding an overall figure of merit of 0.72 have been used to calculate the electron-density map. Molecular models for actin and DNase I derived from this map have dimensions 67 X 40 X 37 A and 50 X 50 X 40 A, respectively. The actin molecule is elongated and consists of a larger and a smaller domain, each containing density regions resembling a central beta-pleated sheet surrounded by alpha-helices. The highest electron-density peak is found in the cleft between the two domains, perhaps indicating the bound ATP. Observed crystal contacts between actin molecules and a model for the F-actin filament are discussed. Two high-affinity Ca2+-binding sites which also bind Ba2+ have been located at the surface of the DNase I molecule.