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| <!--
| | ==Structure of Eugenol Synthase from Ocimum basilicum== |
| The line below this paragraph, containing "STRUCTURE_2qw8", creates the "Structure Box" on the page.
| | <StructureSection load='2qw8' size='340' side='right'caption='[[2qw8]], [[Resolution|resolution]] 1.60Å' scene=''> |
| You may change the PDB parameter (which sets the PDB file loaded into the applet)
| | == Structural highlights == |
| or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| | <table><tr><td colspan='2'>[[2qw8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ocimum_basilicum Ocimum basilicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QW8 FirstGlance]. <br> |
| or leave the SCENE parameter empty for the default display.
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| -->
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| {{STRUCTURE_2qw8| PDB=2qw8 | SCENE= }}
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qw8 OCA], [https://pdbe.org/2qw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qw8 RCSB], [https://www.ebi.ac.uk/pdbsum/2qw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qw8 ProSAT]</span></td></tr> |
| | | </table> |
| '''Structure of Eugenol Synthase from Ocimum basilicum'''
| | == Function == |
| | | [https://www.uniprot.org/uniprot/EGS1_OCIBA EGS1_OCIBA] |
| | | == Evolutionary Conservation == |
| ==Overview== | | [[Image:Consurf_key_small.gif|200px|right]] |
| Phenylpropenes, a large group of plant volatile compounds that serve in multiple roles in defense and pollinator attraction, contain a propenyl side chain. Eugenol synthase (EGS) catalyzes the reductive displacement of acetate from the propenyl side chain of the substrate coniferyl acetate to produce the allyl-phenylpropene eugenol. We report here the structure determination of EGS from basil (Ocimum basilicum) by protein x-ray crystallography. EGS is structurally related to the short-chain dehydrogenase/reductases (SDRs), and in particular, enzymes in the isoflavone-reductase-like subfamily. The structure of a ternary complex of EGS bound to the cofactor NADP(H) and a mixed competitive inhibitor EMDF ((7S,8S)-ethyl (7,8-methylene)-dihydroferulate) provides a detailed view of the binding interactions within the EGS active site and a starting point for mutagenic examination of the unusual reductive mechanism of EGS. The key interactions between EMDF and the EGS-holoenzyme include stacking of the phenyl ring of EMDF against the cofactor's nicotinamide ring and a water-mediated hydrogen-bonding interaction between the EMDF 4-hydroxy group and the side-chain amino moiety of a conserved lysine residue, Lys132. The C4 carbon of nicotinamide resides immediately adjacent to the site of hydride addition, the C7 carbon of cinnamyl acetate substrates. The inhibitor-bound EGS structure suggests a two-step reaction mechanism involving the formation of a quinone-methide prior to reduction. The formation of this intermediate is promoted by a hydrogen-bonding network that favors deprotonation of the substrate's 4-hydroxyl group and disfavors binding of the acetate moiety, akin to a push-pull catalytic mechanism. Notably, the catalytic involvement in EGS of the conserved Lys132 in preparing the phenolic substrate for quinone methide formation through the proton-relay network appears to be an adaptation of the analogous role in hydrogen bonding played by the equivalent lysine residue in other enzymes of the SDR family.
| | Check<jmol> |
| | | <jmolCheckbox> |
| ==About this Structure== | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qw/2qw8_consurf.spt"</scriptWhenChecked> |
| 2QW8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ocimum_basilicum Ocimum basilicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QW8 OCA].
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | | <text>to colour the structure by Evolutionary Conservation</text> |
| ==Reference== | | </jmolCheckbox> |
| Structure and reaction mechanism of basil eugenol synthase., Louie GV, Baiga TJ, Bowman ME, Koeduka T, Taylor JH, Spassova SM, Pichersky E, Noel JP, PLoS ONE. 2007 Oct 3;2(10):e993. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17912370 17912370]
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qw8 ConSurf]. |
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Ocimum basilicum]] | | [[Category: Ocimum basilicum]] |
| [[Category: Single protein]]
| | [[Category: Louie GV]] |
| [[Category: Louie, G V.]] | | [[Category: Noel JP]] |
| [[Category: Noel, J P.]] | |
| [[Category: Eugenol]]
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| [[Category: Oxidoreductase]]
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| [[Category: Phenylpropene]]
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| [[Category: Pip reductase]]
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| [[Category: Plant protein]]
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| [[Category: Short-chain dehydrogenase/reductase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:44:14 2008''
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