5kjt: Difference between revisions

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 <StructureSection load='5kjt' size='340' side='right'caption='[[5kjt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kjt]] 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=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='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=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='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=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>
 == 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/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[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 CF]]
-[[Category: Tung, C F]]
+[[Category: Wang Y]]
-[[Category: Wang, Y]]
+[[Category: Weng JK]]
-[[Category: Weng, J K]]
-[[Category: Acyltransferase]]
-[[Category: Bahd]]
-[[Category: Hct]]
-[[Category: Phenylpropanoid metabolism]]
-[[Category: Transferase]]