1fl2: Difference between revisions
New page: left|200px<br /><applet load="1fl2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fl2, resolution 1.90Å" /> '''CATALYTIC CORE COMPO... |
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[[Image:1fl2.jpg|left|200px]]<br /><applet load="1fl2" size=" | [[Image:1fl2.jpg|left|200px]]<br /><applet load="1fl2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1fl2, resolution 1.90Å" /> | caption="1fl2, resolution 1.90Å" /> | ||
'''CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI'''<br /> | '''CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI'''<br /> | ||
==Overview== | ==Overview== | ||
Alkylhydroperoxide reductases (AhpR, EC 1.6.4.*) are essential for the | 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. | ||
==About this Structure== | ==About this Structure== | ||
1FL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1FL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FL2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bieger, B.]] | [[Category: Bieger, B.]] | ||
[[Category: Essen, L | [[Category: Essen, L O.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: reactive oxygen]] | [[Category: reactive oxygen]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:47 2008'' |
Revision as of 13:39, 21 February 2008
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CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI
OverviewOverview
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.
About this StructureAbout this Structure
1FL2 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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