1fl2: Difference between revisions
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|PDB= 1fl2 |SIZE=350|CAPTION= <scene name='initialview01'>1fl2</scene>, resolution 1.90Å | |PDB= 1fl2 |SIZE=350|CAPTION= <scene name='initialview01'>1fl2</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fl2 OCA], [http://www.ebi.ac.uk/pdbsum/1fl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fl2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Bieger, B.]] | [[Category: Bieger, B.]] | ||
[[Category: Essen, L O.]] | [[Category: Essen, L O.]] | ||
[[Category: alkylhydroperoxide reductase]] | [[Category: alkylhydroperoxide reductase]] | ||
[[Category: disulphide oxidoreductase]] | [[Category: disulphide oxidoreductase]] | ||
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[[Category: reactive oxygen]] | [[Category: reactive oxygen]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:25:05 2008'' | ||
Revision as of 20:25, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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