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| | <StructureSection load='6j95' size='340' side='right'caption='[[6j95]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6j95' size='340' side='right'caption='[[6j95]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j95]] is a 1 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=6J95 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6J95 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j95]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J95 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.002Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP97A3, LUT5, At1g31800, F5M6.19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></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=6j95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j95 OCA], [http://pdbe.org/6j95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j95 RCSB], [http://www.ebi.ac.uk/pdbsum/6j95 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j95 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6j95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j95 OCA], [https://pdbe.org/6j95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j95 RCSB], [https://www.ebi.ac.uk/pdbsum/6j95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j95 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LUT5_ARATH LUT5_ARATH]] Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylation of alpha- and beta-carotene. Has also a low activity toward the epsilon-rings of alpha-carotene. The beta-ring of alpha-carotene is the preferred substrate in planta.<ref>PMID:16492736</ref> <ref>PMID:16890225</ref> <ref>PMID:19147649</ref> | + | [https://www.uniprot.org/uniprot/LUT5_ARATH LUT5_ARATH] Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylation of alpha- and beta-carotene. Has also a low activity toward the epsilon-rings of alpha-carotene. The beta-ring of alpha-carotene is the preferred substrate in planta.<ref>PMID:16492736</ref> <ref>PMID:16890225</ref> <ref>PMID:19147649</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, Q]] | + | [[Category: Guo Q]] |
| - | [[Category: Niu, G]] | + | [[Category: Niu G]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Zhao, S]] | + | [[Category: Zhao S]] |
| - | [[Category: Carotenoid]]
| + | |
| - | [[Category: Lutein biosynthesis]]
| + | |
| - | [[Category: Monooxygenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: P450]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
Function
LUT5_ARATH Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylation of alpha- and beta-carotene. Has also a low activity toward the epsilon-rings of alpha-carotene. The beta-ring of alpha-carotene is the preferred substrate in planta.[1] [2] [3]
Publication Abstract from PubMed
Two cytochrome P450 enzymes, CYP97A3 and CYP97C1, catalyze hydroxylations of the beta- and epsilon-rings of alpha-carotene to produce lutein. Chirality is introduced at the C-3 atom of both rings, and the reactions are both pro-3R-stereospecific. We determined the crystal structures of CYP97A3 in substrate-free and complex forms with a nonnatural substrate and the structure of CYP97C1 in a detergent-bound form. The structures of CYP97A3 in different states show the substrate channel and the structure of CYP97C1 bound with octylthioglucoside confirms the binding site for the carotenoid substrate. Biochemical assays confirm that the ferredoxin-NADP(+) reductase (FNR)-ferredoxin pair is used as the redox partner. Details of the pro-3R stereospecificity are revealed in the retinal-bound CYP97A3 structure. Further analysis indicates that the CYP97B clan bears similarity to the beta-ring-specific CYP97A clan. Overall, our research describes the molecular basis for the last steps of lutein biosynthesis.
Structural basis for plant lutein biosynthesis from alpha-carotene.,Niu G, Guo Q, Wang J, Zhao S, He Y, Liu L Proc Natl Acad Sci U S A. 2020 Jun 23;117(25):14150-14157. doi:, 10.1073/pnas.2001806117. Epub 2020 Jun 8. PMID:32513704[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim J, DellaPenna D. Defining the primary route for lutein synthesis in plants: the role of Arabidopsis carotenoid beta-ring hydroxylase CYP97A3. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3474-9. doi:, 10.1073/pnas.0511207103. Epub 2006 Feb 21. PMID:16492736 doi:http://dx.doi.org/10.1073/pnas.0511207103
- ↑ Fiore A, Dall'osto L, Fraser PD, Bassi R, Giuliano G. Elucidation of the beta-carotene hydroxylation pathway in Arabidopsis thaliana. FEBS Lett. 2006 Aug 21;580(19):4718-22. doi: 10.1016/j.febslet.2006.07.055. Epub , 2006 Jul 26. PMID:16890225 doi:http://dx.doi.org/10.1016/j.febslet.2006.07.055
- ↑ Kim J, Smith JJ, Tian L, Dellapenna D. The evolution and function of carotenoid hydroxylases in Arabidopsis. Plant Cell Physiol. 2009 Mar;50(3):463-79. doi: 10.1093/pcp/pcp005. Epub 2009 Jan, 15. PMID:19147649 doi:http://dx.doi.org/10.1093/pcp/pcp005
- ↑ Niu G, Guo Q, Wang J, Zhao S, He Y, Liu L. Structural basis for plant lutein biosynthesis from alpha-carotene. Proc Natl Acad Sci U S A. 2020 Jun 23;117(25):14150-14157. doi:, 10.1073/pnas.2001806117. Epub 2020 Jun 8. PMID:32513704 doi:http://dx.doi.org/10.1073/pnas.2001806117
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