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| ==Annotations {{HelpIcon|Help:Literature}}== | | ==Annotations {{HelpIcon|Help:Literature}}== |
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| {| id="I47a9935299f5d" class=" tableEdit GO_table_reference dataTable"
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| !|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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| [[ahpF:Gene_Product(s)]], alkyl hydroperoxide reductase
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| GO:0070402
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| NADPH binding
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| ISM: Inferred from Sequence Model
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| UniProtKB:Q39243
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| F
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| The structure of the AhpF catalytic core (residues A212-A521) was solved by molecular replacement using AMoRe and the structure of the plant Arabidopsis thaliana thioredoxin reductase (PDB code 1VDC) as search model. The
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| high quality of the 1.9 Å 2F(obs)- F(calc) electron density map
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| allowed semi-automatic tracing and model rebuilding by WARP and was continuous for the entire protein moiety of the E. coli AhpF. Further re®nement was carried out using
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| CNS until the refinement converged at a R-factor/R-free of 0.197/0.217 for data between 10.0 Å and 1.9 Å. Statistics shown in Table 1.
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| The E. coli and A. thaliana NADPH domains (38 %, 32% sequence identity) superimpose on the AhpF NADPH domain with an r.m.s.d. value of 1.02 and 0.96 AÊ for 119 Ca positions, respectively. As the catalytic core of AhpF was crystallised under oxidizing conditions in the absence of extraneously added NADPH, the
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| NADPH domain lacks a bound NADPH cofactor.
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| [[ahpF:Gene_Product(s)]], alkyl hydroperoxide reductase
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| GO:0050660
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| flavin adenine dinucleotide binding
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| ISM: Inferred from Sequence Model
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| UniProtKB:Q39243
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| F
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| The structure of the AhpF catalytic core (residues A212-A521) was solved by molecular replacement using AMoRe and the structure of the plant Arabidopsis thaliana thioredoxin reductase (PDB code 1VDC) as search model. The
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| high quality of the 1.9 Å 2F(obs)- F(calc) electron density map
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| allowed semi-automatic tracing and model rebuilding by WARP and was continuous for the entire protein moiety of the E. coli AhpF. Further re®nement was carried out using
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| CNS until the refinement converged at a R-factor/R-free of 0.197/0.217 for data between 10.0 Å and 1.9 Å. Statistics shown in Table 1.
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| |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=63ce1649aab8b3180235b0af7618f667.0.I47a9935299f5d&page=120067&pagename={{FULLPAGENAMEE}}&type=0&template=GO_table_reference edit table]</span> || || || || || || || ||
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| ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == |
| Citation
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No author listed (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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| Abstract
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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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| Links
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PubMed
Online version:10.1006/jmbi.2000.4441
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| Keywords
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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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