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

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.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-B073-1 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0001-1937-6
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PNAS_78_1981_4319.pdf (beliebiger Volltext), 2MB
 
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 Urheber:
Suck, Dietrich, Autor
Kabsch, Wolfgang1, 2, Autor           
Mannherz, Hans Georg1, Autor           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Sprache(n): eng - English
 Datum: 1981-07-011981-07-151981
 Publikationsstatus: Erschienen
 Seiten: 5
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.78.7.4319
URI: https://www.ncbi.nlm.nih.gov/pubmed/6270671
URI: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC319781/
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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proceedings of the National Academy of Sciences of the USA
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 78 (7) Artikelnummer: - Start- / Endseite: 4319 - 4323 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230