Structural highlights
Function
AHPF_ECOLI Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A 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.
Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli.,Bieger B, Essen LO J Mol Biol. 2001 Mar 16;307(1):1-8. PMID:11243797[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bieger B, Essen LO. Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli. J Mol Biol. 2001 Mar 16;307(1):1-8. PMID:11243797 doi:10.1006/jmbi.2000.4441
