6j94

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<StructureSection load='6j94' size='340' side='right'caption='[[6j94]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='6j94' size='340' side='right'caption='[[6j94]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6j94]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J94 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6j94]] is a 2 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=6J94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J94 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.401&#8491;</td></tr>
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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=6j94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j94 OCA], [http://pdbe.org/6j94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j94 RCSB], [http://www.ebi.ac.uk/pdbsum/6j94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j94 ProSAT]</span></td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6j94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j94 OCA], [https://pdbe.org/6j94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j94 RCSB], [https://www.ebi.ac.uk/pdbsum/6j94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j94 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:32513704</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6j94" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Guo, Q]]
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[[Category: Guo Q]]
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[[Category: Niu, G]]
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[[Category: Niu G]]
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[[Category: Wang, J]]
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[[Category: Wang J]]
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[[Category: Zhao, S]]
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[[Category: Zhao S]]
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[[Category: Carotenoid]]
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[[Category: Lutein biosynthesis]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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[[Category: P450]]
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[[Category: Photosynthesis]]
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Current revision

Crystal structure of CYP97A3

PDB ID 6j94

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