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5kjw

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==Crystal structure of Coleus blumei HCT in complex with 3-hydroxyacetophenone==
==Crystal structure of Coleus blumei HCT in complex with 3-hydroxyacetophenone==
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<StructureSection load='5kjw' size='340' side='right' caption='[[5kjw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5kjw' size='340' side='right'caption='[[5kjw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kjw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KJW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kjw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plectranthus_scutellarioides Plectranthus scutellarioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=53C:1-(3-HYDROXYPHENYL)ETHANONE'>53C</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kjv|5kjv]]</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=53C:1-(3-HYDROXYPHENYL)ETHANONE'>53C</scene></td></tr>
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<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>
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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=5kjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjw OCA], [https://pdbe.org/5kjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kjw RCSB], [https://www.ebi.ac.uk/pdbsum/5kjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjw ProSAT]</span></td></tr>
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<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=5kjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjw OCA], [http://pdbe.org/5kjw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjw RCSB], [http://www.ebi.ac.uk/pdbsum/5kjw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjw ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/E8ZAP2_PLESU E8ZAP2_PLESU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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 5kjw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Shikimate O-hydroxycinnamoyltransferase]]
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[[Category: Large Structures]]
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[[Category: Chiang, Y C]]
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[[Category: Plectranthus scutellarioides]]
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[[Category: Levsh, O]]
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[[Category: Chiang YC]]
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[[Category: Noel, J P]]
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[[Category: Levsh O]]
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[[Category: Tung, C F]]
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[[Category: Noel JP]]
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[[Category: Wang, Y]]
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[[Category: Tung CF]]
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[[Category: Weng, J K]]
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[[Category: Wang Y]]
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[[Category: Acyltransferase]]
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[[Category: Weng JK]]
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[[Category: Bahd]]
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[[Category: Hct]]
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[[Category: Phenylpropanoid metabolism]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Coleus blumei HCT in complex with 3-hydroxyacetophenone

PDB ID 5kjw

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