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==Crystal structure of Arabidopsis thaliana HCT in complex with p-coumaroyl-CoA==
==Crystal structure of Arabidopsis thaliana HCT in complex with p-coumaroyl-CoA==
<StructureSection load='5kjt' size='340' side='right' caption='[[5kjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5kjt' size='340' side='right'caption='[[5kjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5kjt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJT FirstGlance]. <br>
<table><tr><td colspan='2'>[[5kjt]] is a 1 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=5KJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WCA:P-COUMAROYL-COA'>WCA</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]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kjs|5kjs]], [[5kju|5kju]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WCA:P-COUMAROYL-COA'>WCA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_O-hydroxycinnamoyltransferase Shikimate O-hydroxycinnamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.133 2.3.1.133] </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=5kjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjt OCA], [https://pdbe.org/5kjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kjt RCSB], [https://www.ebi.ac.uk/pdbsum/5kjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjt ProSAT]</span></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=5kjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjt OCA], [http://pdbe.org/5kjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjt RCSB], [http://www.ebi.ac.uk/pdbsum/5kjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HST_ARATH HST_ARATH]] Acyltransferase involved in the biosynthesis of lignin. Accepts caffeoyl-CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on both shikimate and quinate acceptors.<ref>PMID:15161961</ref> 
[https://www.uniprot.org/uniprot/HST_ARATH HST_ARATH] Acyltransferase involved in the biosynthesis of lignin. Accepts caffeoyl-CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on both shikimate and quinate acceptors.<ref>PMID:15161961</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyltransferase (HCT) is an essential acyltransferase that mediates flux through plant phenylpropanoid metabolism by catalyzing a reaction between p-coumaroyl-CoA and shikimate, yet it also exhibits broad substrate permissiveness in vitro. How do enzymes like HCT avoid functional derailment by cellular metabolites that qualify as non-native substrates? Here, we combine X-ray crystallography and molecular dynamics to reveal distinct dynamic modes of HCT under native and non-native catalysis. We find that essential electrostatic and hydrogen-bonding interactions between the ligand and active site residues, permitted by active site plasticity, are elicited more effectively by shikimate than by other non-native substrates. This work provides a structural basis for how dynamic conformational states of HCT favor native over non-native catalysis by reducing the number of futile encounters between the enzyme and shikimate.
 
Dynamic Conformational States Dictate Selectivity toward the Native Substrate in a Substrate-Permissive Acyltransferase.,Levsh O, Chiang YC, Tung CF, Noel JP, Wang Y, Weng JK Biochemistry. 2016 Nov 2. PMID:27805809<ref>PMID:27805809</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kjt" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Shikimate O-hydroxycinnamoyltransferase]]
[[Category: Arabidopsis thaliana]]
[[Category: Chiang, Y C]]
[[Category: Large Structures]]
[[Category: Levsh, O]]
[[Category: Chiang YC]]
[[Category: Noel, J P]]
[[Category: Levsh O]]
[[Category: Tung, C F]]
[[Category: Noel JP]]
[[Category: Wang, Y]]
[[Category: Tung CF]]
[[Category: Weng, J K]]
[[Category: Wang Y]]
[[Category: Acyltransferase]]
[[Category: Weng JK]]
[[Category: Bahd]]
[[Category: Hct]]
[[Category: Phenylpropanoid metabolism]]
[[Category: Transferase]]

Latest revision as of 15:40, 6 March 2024

Crystal structure of Arabidopsis thaliana HCT in complex with p-coumaroyl-CoACrystal structure of Arabidopsis thaliana HCT in complex with p-coumaroyl-CoA

Structural highlights

5kjt is a 1 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 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HST_ARATH Acyltransferase involved in the biosynthesis of lignin. Accepts caffeoyl-CoA and p-coumaroyl-CoA as substrates and transfers the acyl group on both shikimate and quinate acceptors.[1]

References

  1. ↑ Hoffmann L, Besseau S, Geoffroy P, Ritzenthaler C, Meyer D, Lapierre C, Pollet B, Legrand M. Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis. Plant Cell. 2004 Jun;16(6):1446-65. Epub 2004 May 25. PMID:15161961 doi:http://dx.doi.org/10.1105/tpc.020297

5kjt, resolution 2.50Å

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