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| | ==Cystal structure of Arabidopsis ATR2== | | ==Cystal structure of Arabidopsis ATR2== |
| - | <StructureSection load='5gxu' size='340' side='right' caption='[[5gxu]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5gxu' size='340' side='right'caption='[[5gxu]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gxu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GXU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gxu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GXU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> |
| | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH--hemoprotein_reductase NADPH--hemoprotein reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.4 1.6.2.4] </span></td></tr> | | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH--hemoprotein_reductase NADPH--hemoprotein reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.4 1.6.2.4] </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=5gxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxu OCA], [http://pdbe.org/5gxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gxu RCSB], [http://www.ebi.ac.uk/pdbsum/5gxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxu ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxu OCA], [http://pdbe.org/5gxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gxu RCSB], [http://www.ebi.ac.uk/pdbsum/5gxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5gxu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5gxu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Arath]] |
| | + | [[Category: Large Structures]] |
| | [[Category: NADPH--hemoprotein reductase]] | | [[Category: NADPH--hemoprotein reductase]] |
| | [[Category: Liu, L]] | | [[Category: Liu, L]] |
| Structural highlights
Function
[NCPR2_ARATH] 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. Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and dichloroindophenol.[HAMAP-Rule:MF_03212][1] [2] [3] [4] [5]
Publication Abstract from PubMed
Members of the cytochrome P450 family catalyze a variety of mono-oxygenase reactions, and for the eukaryotic membrane-bound members, NADPH is typically used as the reducing agent. The flavoprotein NADPH-cytochrome P450 reductase (CPR) enables electron transfer from NADPH to cytochrome P450 via its flavin cofactors. ATR2 is one of the two authentic CPR genes in the genome of the model plant Arabidopsis thaliana, and its product has been physiologically and kinetically characterized. Here, we report the 2.3 A structure of Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) and find that the position of the two flavin cofactors differs from that of other known CPR structures. Mutation of residues related to possible interflavin electron transfer retains the reductase activity of ATR2, which suggests a direct electron transfer pathway between the flavins. In contrast, mutation of a single residue (R708) mediating interdomain interaction abolishes this activity. Because this residue is only conserved in plant CPRs, we speculate a plant-specific working mechanism as observed in ATR2. DATABASE: Atomic coordinates and structure factors of ATR2 are available in the Protein Data Bank under the accession code 5GXU.
Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.,Niu G, Zhao S, Wang L, Dong W, Liu L, He Y FEBS J. 2017 Mar;284(5):754-765. doi: 10.1111/febs.14017. Epub 2017 Feb 8. PMID:28103421[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hull AK, Celenza JL. Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2. Protein Expr Purif. 2000 Apr;18(3):310-5. PMID:10733884 doi:http://dx.doi.org/10.1006/prep.1999.1195
- ↑ Urban P, Mignotte C, Kazmaier M, Delorme F, Pompon D. Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5. J Biol Chem. 1997 Aug 1;272(31):19176-86. PMID:9235908
- ↑ Mizutani M, Ohta D. Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation. Plant Physiol. 1998 Jan;116(1):357-67. PMID:9449848
- ↑ Fukuchi-Mizutani M, Mizutani M, Tanaka Y, Kusumi T, Ohta D. Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis. Plant Physiol. 1999 Jan;119(1):353-62. PMID:9880378
- ↑ Louerat-Oriou B, Perret A, Pompon D. Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities. Eur J Biochem. 1998 Dec 15;258(3):1040-9. PMID:9990323
- ↑ Niu G, Zhao S, Wang L, Dong W, Liu L, He Y. Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function. FEBS J. 2017 Mar;284(5):754-765. doi: 10.1111/febs.14017. Epub 2017 Feb 8. PMID:28103421 doi:http://dx.doi.org/10.1111/febs.14017
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