Crystallization and preliminary X-ray analysis of the catalytic core of the alkylhydroperoxide reductase component AhpF from Escherichia coli.
Acta Crystallogr D Biol Crystallogr
; 56(Pt 1): 92-4, 2000 Jan.
Article
em En
| MEDLINE
| ID: mdl-10666639
ABSTRACT
Alkylhydroperoxide reductases (AhpR, E.C. 1.6.4.x) are essential for the oxygen tolerance of aerobic organisms, converting otherwise toxic hydroperoxides of lipids or nucleic acids to their corresponding alcohols. The AhpF component (521 amino-acid residues, 56.2 kDa) belongs to the family of pyridine nucleotide-disulfide oxidoreductases and channels electrons from NAD(P)H via a series of disulfides towards the AhpC component, which finally reduces the hydro-peroxide substrates. Crystals of the proteolytically truncated AhpF component (residues Asn208-Ala521) of the alkyl hydroperoxide reductase from Escherichia coli were grown under oxidizing conditions. The crystals belong to space group P3(2)21, with unit-cell parameters a = 60.4, c = 171.8 A. X-ray diffraction data were collected to 1.9 A resolution using synchrotron radiation. A molecular-replacement solution was found using the structure of thioredoxin reductase from Arabidopsis thaliana as a search model.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
/
Escherichia coli
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Alemanha