5kjt: Difference between revisions

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<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 [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>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WCA:P-COUMAROYL-COA'>WCA</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kjs|5kjs]], [[5kju|5kju]]</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='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='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>
<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>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Shikimate O-hydroxycinnamoyltransferase]]
[[Category: Shikimate O-hydroxycinnamoyltransferase]]
[[Category: Chiang, Y C]]
[[Category: Chiang, Y C]]

Revision as of 21:22, 15 November 2017

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 Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:HST, HCT, At5g48930, K19E20.4 (ARATH)
Activity:Shikimate O-hydroxycinnamoyltransferase, with EC number 2.3.1.133
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]

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

  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
  2. 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

5kjt, resolution 2.50Å

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