Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli

被引:17
作者
Bieger, B [1 ]
Essen, LO [1 ]
机构
[1] Max Planck Inst Biochem, Dept Membrane Biochem, D-82152 Martinsried, Germany
关键词
alkylhydroperoxide reductase; disulphide oxidoreductase; reactive oxygen; FAD; crystal structure;
D O I
10.1006/jmbi.2000.4441
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Alkylhydroperoxide reductases (AhpR, EC 1.6.4.*) are essential for the oxygen tolerance of aerobic organisms by converting otherwise toxic hydroperoxides of lipids or nucleic acids to the corresponding alcohols. The AhpF: component belongs to the family of pyridine nucleotide-disulphide oxidoreductases and channels electrons from NAD(P)H towards the AhpC component which finally reduces cognate substrates. The structure of the catalytic core of the Escherichia coli AhpF (A212-A521) with a bound FAD cofactor was determined at 1.9 Angstrom resolution in its oxidized state. The dimeric arrangement of the AhpF catalytic core and the predicted interaction mode between the N-terminal PDO-like domain and the NADPH domain favours an intramolecular electron transfer between the two redox-active disulphide centres of AhpF. (C) 2001 Academic Press.
引用
收藏
页码:1 / 8
页数:8
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