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| | <StructureSection load='5kjs' size='340' side='right'caption='[[5kjs]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5kjs' size='340' side='right'caption='[[5kjs]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kjs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kjs]] 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=5KJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJS FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.203Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kjt|5kjt]], [[5kju|5kju]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HST, HCT, At5g48930, K19E20.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5kjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjs OCA], [https://pdbe.org/5kjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kjs RCSB], [https://www.ebi.ac.uk/pdbsum/5kjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjs ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjs OCA], [http://pdbe.org/5kjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjs RCSB], [http://www.ebi.ac.uk/pdbsum/5kjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjs 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shikimate O-hydroxycinnamoyltransferase]]
| + | [[Category: Chiang YC]] |
| - | [[Category: Chiang, Y C]] | + | [[Category: Levsh O]] |
| - | [[Category: Levsh, O]] | + | [[Category: Noel JP]] |
| - | [[Category: Noel, J P]] | + | [[Category: Tung C]] |
| - | [[Category: Tung, C]] | + | [[Category: Wang Y]] |
| - | [[Category: Wang, Y]] | + | [[Category: Weng JK]] |
| - | [[Category: Weng, J K]] | + | |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Bahd]]
| + | |
| - | [[Category: Phenylpropanoid metabolism]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ Levsh O, Chiang YC, Tung CF, Noel JP, Wang Y, Weng JK. Dynamic Conformational States Dictate Selectivity toward the Native Substrate in a Substrate-Permissive Acyltransferase. Biochemistry. 2016 Nov 2. PMID:27805809 doi:http://dx.doi.org/10.1021/acs.biochem.6b00887
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