Crystallization and preliminary X-ray studies of azoreductases fromBacillussp. B29
| Autor: | Takaaki Fujiwara, Isao Tanaka, Toshihiko Ooi, Min Yao, Daiki Ogata, Seiichi Taguchi |
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| Rok vydání: | 2010 |
| Předmět: |
Stereochemistry
Biophysics Flavoprotein Flavin mononucleotide Bacillus Crystallography X-Ray Biochemistry Cofactor law.invention Crystal chemistry.chemical_compound Structural Biology law Genetics NADH NADPH Oxidoreductases Crystallization Bacillus (shape) chemistry.chemical_classification biology Resolution (electron density) Nitroreductases Condensed Matter Physics biology.organism_classification Crystallography Enzyme chemistry Crystallization Communications biology.protein |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:503-505 |
| ISSN: | 1744-3091 |
| Popis: | Azoreductases from Bacillus sp. B29 are NADH-dependent flavoenzymes which contain a flavin mononucleotide (FMN) as a prosthetic group and exist as homodimers composed of 23 kDa subunits. These enzymes catalyze the reductive degradation of various azo compounds by a ping-pong mechanism. In order to determine the structure-function relationship of the azo-dye reduction mechanism, an X-ray crystallographic study of azoreductases was performed. Selenomethionine-labelled AzrA (SeMet-AzrA) and AzrC were crystallized by the hanging-drop vapour-diffusion method. A crystal of SeMet-AzrA diffracted to 2.0 A resolution and was determined to belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.9, b = 69.0, c = 105.4 A. The native crystals of AzrC belonged to space group C2, with unit-cell parameters a = 192.0, b = 56.6, c = 105.5 A, beta = 115.7 degrees , and diffracted to 2.21 A resolution. |
| Databáze: | OpenAIRE |
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