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5fan

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==Crystal structure of PvHCT in complex with p-coumaroyl-CoA and protocatechuate==
==Crystal structure of PvHCT in complex with p-coumaroyl-CoA and protocatechuate==
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<StructureSection load='5fan' size='340' side='right' caption='[[5fan]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5fan' size='340' side='right'caption='[[5fan]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fan]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FAN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5fan]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Panicum_virgatum Panicum virgatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FAN 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=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=WCA:P-COUMAROYL-COA'>WCA</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]] 1.901&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=WCA:P-COUMAROYL-COA'>WCA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fal|5fal]]</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=5fan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fan OCA], [https://pdbe.org/5fan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fan RCSB], [https://www.ebi.ac.uk/pdbsum/5fan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fan 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=5fan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fan OCA], [http://pdbe.org/5fan PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fan RCSB], [http://www.ebi.ac.uk/pdbsum/5fan PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/R9RYW2_PANVG R9RYW2_PANVG]
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Lignin poses a major challenge in the processing of plant biomass for agro-industrial applications. For bioengineering purposes, there is a pressing interest in identifying and characterizing the enzymes responsible for the biosynthesis of lignin. Hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl transferase (HCT, EC 2.3.1.133) is a key metabolic entry point for the synthesis of the most important lignin monomers: coniferyl and sinapyl alcohols. In this study, we investigated the substrate promiscuity of HCT from a bryophyte (Physcomitrella) and from five representatives of vascular plants (Arabidopsis, poplar, switchgrass, pine, and Selaginella) using a yeast expression system. We demonstrate for these HCTs a conserved capacity to acylate with p-coumaroyl-CoA several phenolic compounds in addition to the canonical acceptor shikimate normally used during lignin biosynthesis. Using either recombinant HCT from switchgrass (PvHCT2a) or an Arabidopsis protein stem extract, we show evidence of the inhibitory effect of these phenolics on the synthesis of p-coumaroyl shikimate in vitro, which presumably occurs via a mechanism of competitive inhibition. Structural study of PvHCT2a confirmed the binding of a non-canonical acceptor in a similar manner as shikimate in the active site of the enzyme. Finally, we exploited in Arabidopsis the substrate flexibility of HCT to reduce lignin content and improve biomass saccharification by engineering transgenic lines that overproduce one of the HCT non-canonical acceptors. Our results demonstrate conservation of HCT substrate promiscuity and provide support for a new strategy for lignin reduction in the effort to improve the quality of plant biomass for forage and cellulosic biofuels.
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Exploiting The Substrate Promiscuity of Hydroxycinnamoyl-CoA:shikimate Hydroxycinnamoyl Transferase to Reduce Lignin.,Eudes A, Pereira JH, Yogiswara S, Wang G, Teixeira Benites V, Baidoo EE, Lee TS, Adams PD, Keasling JD, Loque D Plant Cell Physiol. 2016 Feb 8. pii: pcw016. PMID:26858288<ref>PMID:26858288</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 5fan" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Adams, P D]]
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[[Category: Large Structures]]
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[[Category: Baidoo, E E.K]]
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[[Category: Panicum virgatum]]
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[[Category: Benites, V T]]
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[[Category: Adams PD]]
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[[Category: Eudes, A]]
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[[Category: Baidoo EEK]]
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[[Category: Keasling, J D]]
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[[Category: Benites VT]]
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[[Category: Lee, T S]]
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[[Category: Eudes A]]
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[[Category: Loque, D]]
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[[Category: Keasling JD]]
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[[Category: Moriarty, N W]]
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[[Category: Lee TS]]
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[[Category: Pereira, J H]]
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[[Category: Loque D]]
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[[Category: Wang, G]]
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[[Category: Moriarty NW]]
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[[Category: Yogiswara, S]]
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[[Category: Pereira JH]]
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[[Category: Transferase]]
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[[Category: Wang G]]
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[[Category: Yogiswara S]]

Current revision

Crystal structure of PvHCT in complex with p-coumaroyl-CoA and protocatechuate

PDB ID 5fan

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