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  Three-dimensional structure of the complex of actin and DNase I at 4.5 A resolution

Kabsch, W., Mannherz, H. G., & Suck, D. (1985). Three-dimensional structure of the complex of actin and DNase I at 4.5 A resolution. EMBO Journal, 4(8), 2113-2118. doi:10.1002/j.1460-2075.1985.tb03900.x.

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 Urheber:
Kabsch, Wolfgang1, 2, Autor           
Mannherz, Hans Georg1, Autor           
Suck, Dietrich, 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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Schlagwörter: actin/DNase I/X-ray; structure
 Zusammenfassung: The shape of an actin subunit has been derived from an improved 6 A map of the complex of rabbit skeletal muscle actin and bovine pancreatic DNase I obtained by X-ray crystallographic methods. The three-dimensional structure of DNase I determined independently at 2.5 A resolution was compared with the DNase I electron density in the actin:DNase map. The two structures are very similar at 6 A resolution thus leading to an unambiguous identification of actin as well as DNase I electron density. Furthermore the correct hand of the actin structure is determined from the DNase I atomic structure. The resolution of the actin structure was extended to 4.5 A by using a single heavy-atom derivative and the knowledge of the atomic coordinates of DNase I. The dimensions of an actin subunit are 67 A X 40 A X 37 A. It consists of a small and a large domain, the small domain containing the N terminus. Actin is an alpha,beta-protein with a beta-pleated sheet in each domain. These sheets are surrounded by several alpha-helices, comprising at least 40% of the structure. The phosphate peak of the adenine nucleotide is located between the two domains. The complex of actin and DNase I as found in solution (i.e., the actin:DNase I contacts which do not depend on crystal packing) was deduced from a comparison of monoclinic with orthorhombic crystals. Residues 44-46, 51, 52, 60-62 of DNase I are close to a loop region in the small domain of actin. At a distance of approximately 15 A there is a second contact in the large domain in which Glu13 of DNase I is involved. A possible binding region for myosin is discussed.

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Sprache(n): eng - English
 Datum: 1985-05-201985-08
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
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Titel: EMBO Journal
  Andere : EMBO J.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Nature Publishing Group
Seiten: - Band / Heft: 4 (8) Artikelnummer: - Start- / Endseite: 2113 - 2118 Identifikator: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061