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• W73520667 abstract "Research Article1 August 1985free access Three-dimensional structure of the complex of actin and DNase I at 4.5 A resolution. W. Kabsch W. Kabsch Search for more papers by this author H.G. Mannherz H.G. Mannherz Search for more papers by this author D. Suck D. Suck Search for more papers by this author W. Kabsch W. Kabsch Search for more papers by this author H.G. Mannherz H.G. Mannherz Search for more papers by this author D. Suck D. Suck Search for more papers by this author Author Information W. Kabsch, H.G. Mannherz and D. Suck The EMBO Journal (1985)4:2113-2118https://doi.org/10.1002/j.1460-2075.1985.tb03900.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 4Issue 81 August 1985In this issue RelatedDetailsLoading ..." @default.
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• W73520667 title "Three-dimensional structure of the complex of actin and DNase I at 4.5 A resolution." @default.
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• W73520667 doi "https://doi.org/10.1002/j.1460-2075.1985.tb03900.x" @default.
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