1fl2

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{{STRUCTURE_1fl2| PDB=1fl2 | SCENE= }}
{{STRUCTURE_1fl2| PDB=1fl2 | SCENE= }}
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'''CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI'''
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===CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 11243797 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11243797}}
==About this Structure==
==About this Structure==
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[[Category: Fad]]
[[Category: Fad]]
[[Category: Reactive oxygen]]
[[Category: Reactive oxygen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:27:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:25:35 2008''

Revision as of 00:25, 1 July 2008

Image:1fl2.png

Template:STRUCTURE 1fl2

CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI

Template:ABSTRACT PUBMED 11243797

About this Structure

1FL2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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