1FL2

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

Summary for 1FL2

• Entry DOI: 10.2210/pdb1fl2/pdb
• Descriptor: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: alkylhydroperoxide reductase, reactive oxygen, fad, disulphide oxidoreductase, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 34197.40

Authors

Bieger, B.,Essen, L.-O. (deposition date: 2000-08-11, release date: 2001-03-21, Last modification date: 2024-10-09)

Primary citation

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

PubMed 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.

PubMed: 11243797
DOI: 10.1006/jmbi.2000.4441

Experimental method

X-RAY DIFFRACTION (1.9 Å)