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NADPH-Cytochrome P450 Reductase
From Proteopedia
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| - | + | <StructureSection load='' size='350' side='right' caption='Human NADPH-Cytochrome P450 reductase FMN-binding and FAD/NADPH domains complex with FMN, FAD, NADP and Ca+2 ion (green) (PDB entry [[3qe2]])' scene='43/436100/Cv/2'> | |
| + | __TOC__ | ||
| + | == Function == | ||
| - | [[NADPH-Cytochrome P450 Reductase]] (P450r) is the electron donor for several oxygenase enzymes including Cytochrome P450<ref>PMID:19171935</ref>. | + | [[NADPH-Cytochrome P450 Reductase]] (P450r) or '''NADPH cytochrome P450 oxidoreductase''' is the electron donor for several oxygenase enzymes including Cytochrome P450<ref>PMID:19171935</ref>. |
See also [[NADPH Cytochrome P450 Oxidoreductase]]. | See also [[NADPH Cytochrome P450 Oxidoreductase]]. | ||
| + | == Disease == | ||
| + | Mutations in P450r resulting in its deficiency are observed in many steroid metabolizing diseases and in skeletal malformation<ref>PMID:23353702</ref>. | ||
| + | |||
| + | == Structural highlights == | ||
| + | P450r electron transfer cofactors: <scene name='43/436100/Cv/18'>FMN, FAD, NADPH are all in proximity</scene><ref>PMID:21808038</ref>. | ||
| + | *<scene name='43/436100/Cv/19'>NADP binding site</scene>. Water molecule are shown as red spheres. | ||
| + | *<scene name='43/436100/Cv/20'>FAD/NADP connection via Thr538 and water molecule</scene>. | ||
| + | *<scene name='43/436100/Cv/21'>FAD binding site</scene>. | ||
| + | *<scene name='43/436100/Cv/22'>FAD and FMN are also in proximity</scene>. | ||
| + | *<scene name='43/436100/Cv/23'>FMN binding site</scene>. | ||
| + | *<scene name='43/436100/Cv/24'>NADP and FAD are in pockets, while FMN is in tunnel</scene>. | ||
| + | </StructureSection> | ||
== 3D Structures of NADPH-Cytochrome P450 Reductase == | == 3D Structures of NADPH-Cytochrome P450 Reductase == | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *P450r | + | *P450r FMN-binding domain (residues 61-241) |
| - | **[[ | + | **[[1b1c]] - hP450r + FMN - human<br /> |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | *P450r | + | *P450r FAD/NADPH domain (residues 241-677) |
| - | **[[ | + | **[[3qfs]] – hP450r + FAD + NADP<br /> |
| + | **[[3qft]] - hP450r (mutant) + FAD + NADP<br /> | ||
| - | *P450r | + | *P450r FMN-binding and FAD/NADPH domains (residues 64-677) |
| - | **[[1amo]] - rP450r <br /> | + | **[[3qe2]], [[5fa6]] – hP450r + FAD + FMN + NADP<br /> |
| - | **[[ | + | **[[3qfc]], [[3qfr]], [[5emn]] – hP450r (mutant) + FAD + FMN + NADP<br /> |
| - | **[[ | + | **[[3es9]], [[1ja0]], [[5urd]], [[5ure]], [[5urg]] - rP450r + FAD + FMN + NADP - rat<br /> |
| + | **[[1j9z]], [[1ja1]], [[4y7c]], [[4y9r]], [[4y9u]], [[5urh]], [[6njr]], [[7l18]] - rP450r (mutant) + FAD + FMN + NADP<br / > | ||
| + | **[[4yaf]], [[4yal]] - rP450r + FAD + FMN + AMP<br / > | ||
| + | **[[4yaw]], [[4yao]], [[4yau]], [[5uri]] - rP450r (mutant) + FAD + FMN + AMP<br / > | ||
| + | **[[3ojw]], [[3ojx]] - rP450r (mutant) + FAD + FMN<br / > | ||
| + | **[[3wkt]] - rP450r (mutant) + heme oxygenase 1 + FAD + FMN + NADP + heme<br /> | ||
| + | **[[1amo]] - rP450r + FAD + FMN + NADP<br /> | ||
| + | **[[6njr]] - rP450r (mutant) + FAD + FMN + NADP + pyrrolydine derivative<br /> | ||
| + | **[[2bpo]] - yP450r (mutant) + FAD + FMN + NADP - yeast<br /> | ||
| + | **[[2bf4]], [[2bn4]] - yP450r + FAD + FMN + NADP<br /> | ||
| + | **[[3fjo]] – yP450r/hP450r + FAD + FMN<br /> | ||
| - | *P450r FAD/ | + | *P450r |
| + | |||
| + | **[[7sux]], [[7sv0]] – sP450r + FAD + NADP - sorghum<br /> | ||
| + | **[[7suz]] – sP450r + FAD <br /> | ||
| + | **[[5ucw]] - P450r (mutant) – ''Bacillus megaterium''<br /> | ||
| + | **[[5gxu]] - P450r + FAD + FMN – ''Arabidopsis thaliana''<br /> | ||
| + | **[[6t1u]] - CtP450r + FAD + FMN – ''Candida tropicalis''<br /> | ||
| + | **[[6t1t]] - CtP450r + FAD + FMN + NADP <br /> | ||
| - | **[[3qfs]] – hP450r<br /> | ||
| - | **[[3qft]] - hP450r (mutant)<br /> | ||
| - | **[[3fjo]] – yP450r/hP450r <br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of NADPH-Cytochrome P450 Reductase
Updated on 11-July-2023
References
- ↑ Hamdane D, Xia C, Im SC, Zhang H, Kim JJ, Waskell L. Structure and function of an NADPH-cytochrome P450 oxidoreductase in an open conformation capable of reducing cytochrome P450. J Biol Chem. 2009 Apr 24;284(17):11374-84. Epub 2009 Jan 26. PMID:19171935 doi:10.1074/jbc.M807868200
- ↑ Pandey AV, Fluck CE. NADPH P450 oxidoreductase: structure, function, and pathology of diseases. Pharmacol Ther. 2013 May;138(2):229-54. doi: 10.1016/j.pharmthera.2013.01.010., Epub 2013 Jan 24. PMID:23353702 doi:http://dx.doi.org/10.1016/j.pharmthera.2013.01.010
- ↑ Xia C, Panda SP, Marohnic CC, Martasek P, Masters BS, Kim JJ. Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency. Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):13486-91. Epub 2011 Aug 1. PMID:21808038 doi:10.1073/pnas.1106632108
