4xae

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(New page: '''Unreleased structure''' The entry 4xae is ON HOLD until sometime in the future Authors: Zhou, D., Kandavelu, P., Zhang, H., WANG, B.C., ROSE, J., YAN, Y. Description: STRUCTURE OF F...)
Current revision (07:42, 27 September 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4xae is ON HOLD until sometime in the future
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==Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana==
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<StructureSection load='4xae' size='340' side='right'caption='[[4xae]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xae]] 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=4XAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XAE FirstGlance]. <br>
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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]] 2.769&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4xae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xae OCA], [https://pdbe.org/4xae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xae RCSB], [https://www.ebi.ac.uk/pdbsum/4xae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xae ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/F6H1_ARATH F6H1_ARATH] 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD)involved in scopoletin biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA but has no activity with ferulic acid, feruloylquinic acid, caffeic acid, caffeoyl CoA, p-coumaric acid, cinnamic acid, cinnamoyl CoA or benzoyl CoA.<ref>PMID:18547395</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Coumarins belong to an important class of plant secondary metabolites. Feruloyl-CoA 6'-hydroxylase (F6'H), a 2-oxoglutarate dependent dioxygenase (2OGD), catalyzes a pivotal step in the biosynthesis of a simple coumarin scopoletin. In this study, we determined the 3-dimensional structure of the F6'H1 apo enzyme by X-ray crystallography. It is the first reported structure of a 2OGD enzyme involved in coumarin biosynthesis and closely resembles the structure of Arabidopsis thaliana anthocyanidin synthase. To better understand the mechanism of enzyme catalysis and substrate specificity, we also generated a homology model of a related ortho-hydroxylase (C2'H) from sweet potato. By comparing these two structures, we targeted two amino acid residues and verified their roles in substrate binding and specificity by site-directed mutagenesis.
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Authors: Zhou, D., Kandavelu, P., Zhang, H., WANG, B.C., ROSE, J., YAN, Y.
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Structural Insights into Substrate Specificity of Feruloyl-CoA 6'-Hydroxylase from Arabidopsis thaliana.,Sun X, Zhou D, Kandavelu P, Zhang H, Yuan Q, Wang BC, Rose J, Yan Y Sci Rep. 2015 May 20;5:10355. doi: 10.1038/srep10355. PMID:25993561<ref>PMID:25993561</ref>
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Description: STRUCTURE OF Feruloyl-CoA 6-hydroxylase (F6H) FROM Arabidopsis thaliana
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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 4xae" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arabidopsis thaliana]]
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[[Category: Large Structures]]
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[[Category: Kandavelu P]]
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[[Category: Rose J]]
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[[Category: Wang BC]]
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[[Category: Yan Y]]
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[[Category: Zhang H]]
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[[Category: Zhou D]]

Current revision

Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana

PDB ID 4xae

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