PMID:11243797: Difference between revisions

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<span style = 'font-size: large'> '''Bieger, B and Essen, LO'''  (2001) Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli.''J. Mol. Biol.'' '''307''':1-8</span>
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|{{TableHeadingColor}} |'''Abstract''' || 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.
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'''Bieger, B and Essen, LO'''  (2001) Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli. ''J. Mol. Biol.'' '''307''':1-8
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11243797 PubMed]
Online version:[http://dx.doi.org/10.1006/jmbi.2000.4441 10.1006/jmbi.2000.4441]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11243797 PubMed]
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Catalytic Domain; Crystallography, X-Ray; Disulfides/chemistry; Electron Transport; Escherichia coli/enzymology; Escherichia coli Proteins; Flavin-Adenine Dinucleotide/chemistry; Models, Molecular; Oxidation-Reduction; Peroxidases/chemistry; Peroxiredoxins; Protein Conformation
 
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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Latest revision as of 04:14, 15 September 2013

Citation

Bieger, B and Essen, LO (2001) Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli. J. Mol. Biol. 307:1-8

Abstract

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.

Links

PubMed Online version:10.1006/jmbi.2000.4441

Keywords

Catalytic Domain; Crystallography, X-Ray; Disulfides/chemistry; Electron Transport; Escherichia coli/enzymology; Escherichia coli Proteins; Flavin-Adenine Dinucleotide/chemistry; Models, Molecular; Oxidation-Reduction; Peroxidases/chemistry; Peroxiredoxins; Protein Conformation

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