3fjo: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fjo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fjo RCSB], [http://www.ebi.ac.uk/pdbsum/3fjo PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fjo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fjo RCSB], [http://www.ebi.ac.uk/pdbsum/3fjo PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NCPR_YEAST NCPR_YEAST]] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.<ref>PMID:1730736</ref> <ref>PMID:9368374</ref> <ref>PMID:9468503</ref> <ref>PMID:11485306</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 21:24, 25 December 2014

Structure of chimeric YH CPRStructure of chimeric YH CPR

Structural highlights

3fjo is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:NCP1, POR (Saccharomyces cerevisiae)
Activity:NADPH--hemoprotein reductase, with EC number 1.6.2.4
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[NCPR_YEAST] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase system that participates in the metabolism of endo- and xenobiotic compounds in mammals. Available CPR structures show a closed conformation, with the two cofactors in tight proximity, which is consistent with FAD-to-FMN, but not FMN-to-P450, electron transfer. Here, we report the 2.5 A resolution crystal structure of a functionally competent yeast-human chimeric CPR in an open conformation, compatible with FMN-to-P450 electron transfer. Comparison with closed structures shows a major conformational change separating the FMN and FAD cofactors from 86 A.

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.,Aigrain L, Pompon D, Morera S, Truan G EMBO Rep. 2009 Jul;10(7):742-7. Epub 2009 May 29. PMID:19483672[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Turi TG, Loper JC. Multiple regulatory elements control expression of the gene encoding the Saccharomyces cerevisiae cytochrome P450, lanosterol 14 alpha-demethylase (ERG11). J Biol Chem. 1992 Jan 25;267(3):2046-56. PMID:1730736
  2. ↑ Lesuisse E, Casteras-Simon M, Labbe P. Cytochrome P-450 reductase is responsible for the ferrireductase activity associated with isolated plasma membranes of Saccharomyces cerevisiae. FEMS Microbiol Lett. 1997 Nov 1;156(1):147-52. PMID:9368374
  3. ↑ Venkateswarlu K, Lamb DC, Kelly DE, Manning NJ, Kelly SL. The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity. J Biol Chem. 1998 Feb 20;273(8):4492-6. PMID:9468503
  4. ↑ Lamb DC, Warrilow AG, Venkateswarlu K, Kelly DE, Kelly SL. Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase. Biochem Biophys Res Commun. 2001 Aug 10;286(1):48-54. PMID:11485306 doi:10.1006/bbrc.2001.5338
  5. ↑ Aigrain L, Pompon D, Morera S, Truan G. Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase. EMBO Rep. 2009 Jul;10(7):742-7. Epub 2009 May 29. PMID:19483672 doi:10.1038/embor.2009.82

3fjo, resolution 2.50Å

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