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Three-dimensional structure of actinoxanthin. IV. A 2.5-Å resolution

✍ Scribed by V. Z. Pletnev; A. P. Kuzin; S. D. Trakhanov; P. V. Kostetsky

Publisher
Wiley (John Wiley & Sons)
Year
1982
Tongue
English
Weight
608 KB
Volume
21
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The protein actinoxanthin (isolated from Actinomyces globisporus—molecular weight, 10,300; 107 amino acid residues) crystallizes in space group __P__2~1~2~1~2~1~ with cell dimensions: a = 30.9 Å, b = 48.8 Å, c = 64.1 Å, and Z = 4. The three‐dimensional structure of actinoxanthin was determined by the x‐ray multiple isomorphous replacement method at 2.5‐Å resolution. The molecule is kidney‐shaped and has a well‐defined cavity. Its characteristic features are the absence of α‐helices and the presence of enhanced content of antiparallel β‐structure (∼55%). A cylinder‐shaped formation of seven antiparallel β‐strands comprises the main part of the protein structure. The established β‐supersecondary structure is characterized by a three‐dimensional topology similar to that of immunoglobulin domains, superoxide dismutase subunits, and azurin and plastocyanin proteins.

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