6l8h

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of CYP97C1

Structural highlights

6l8h is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LUT1_ARATH Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for epsilon- and beta-ring hydroxylation of alpha-carotene. Has only a low activity toward the beta-rings of beta-carotene. The preferred substrate in planta is not alpha-carotene but the epsilon-ring of zeinoxanthin.^[1] ^[2] ^[3] ^[4]

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^[5]

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

References

↑ Tian L, Magallanes-Lundback M, Musetti V, DellaPenna D. Functional analysis of beta- and epsilon-ring carotenoid hydroxylases in Arabidopsis. Plant Cell. 2003 Jun;15(6):1320-32. doi: 10.1105/tpc.011403. PMID:12782726 doi:http://dx.doi.org/10.1105/tpc.011403
↑ 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
↑ Kim JE, Cheng KM, Craft NE, Hamberger B, Douglas CJ. Over-expression of Arabidopsis thaliana carotenoid hydroxylases individually and in combination with a beta-carotene ketolase provides insight into in vivo functions. Phytochemistry. 2010 Feb;71(2-3):168-78. doi: 10.1016/j.phytochem.2009.10.011., Epub 2009 Nov 24. PMID:19939422 doi:http://dx.doi.org/10.1016/j.phytochem.2009.10.011
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6l8h"

Categories: Arabidopsis thaliana | Large Structures | Guo Q | Liu L | Niu G

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6l8h is ON HOLD
+==Crystal structure of CYP97C1==
+<StructureSection load='6l8h' size='340' side='right'caption='[[6l8h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6l8h]] is a 4 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=6L8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L8H FirstGlance]. <br>
+</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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SOG:2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>SOG</scene></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=6l8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8h OCA], [https://pdbe.org/6l8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l8h RCSB], [https://www.ebi.ac.uk/pdbsum/6l8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8h ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LUT1_ARATH LUT1_ARATH] Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for epsilon- and beta-ring hydroxylation of alpha-carotene. Has only a low activity toward the beta-rings of beta-carotene. The preferred substrate in planta is not alpha-carotene but the epsilon-ring of zeinoxanthin.<ref>PMID:12782726</ref> <ref>PMID:16890225</ref> <ref>PMID:19147649</ref> <ref>PMID:19939422</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6l8h" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Guo Q]]
+[[Category: Liu L]]
+[[Category: Niu G]]

6l8h

From Proteopedia

Current revision

Crystal structure of CYP97C1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox