4xae: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana== | ||
<StructureSection load='4xae' size='340' side='right' caption='[[4xae]], [[Resolution|resolution]] 2.77Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xae]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XAE FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<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=4xae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xae OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xae RCSB], [http://www.ebi.ac.uk/pdbsum/4xae PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kandavelu, P]] | |||
[[Category: Rose, J]] | |||
[[Category: Wang, B C]] | |||
[[Category: Yan, Y]] | |||
[[Category: Zhang, H]] | [[Category: Zhang, H]] | ||
[[Category: Zhou, D]] | [[Category: Zhou, D]] | ||
[[Category: | [[Category: 2-oxoglutarate dependent dioxygenase]] | ||
[[Category: | [[Category: Coumarin]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Protein engineering]] | |||
Revision as of 16:57, 10 June 2015
Structure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thalianaStructure of Feruloyl-CoA 6-hydroxylase (F6H) from Arabidopsis thaliana
Structural highlights
Function[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.[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
|
| ||||||||||||||||||