4xae: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
</td></tr><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.769Å</td></tr> | ||
<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> | |||
<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> | <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> | ||
</table> | </table> | ||
Latest revision as of 10:42, 27 September 2023
Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thalianaStructure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana
Structural highlights
FunctionF6H1_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.[1] Publication Abstract from PubMedCoumarins 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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