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3tky

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Current revision (13:32, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tky' size='340' side='right'caption='[[3tky]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
<StructureSection load='3tky' size='340' side='right'caption='[[3tky]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tky]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clabr Clabr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tky]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clarkia_breweri Clarkia breweri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TKY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=N7I:4-[(1E)-3-HYDROXYPROP-1-EN-1-YL]-2-METHOXYPHENOL'>N7I</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.47&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IEMT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36903 CLABR])</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=N7I:4-[(1E)-3-HYDROXYPROP-1-EN-1-YL]-2-METHOXYPHENOL'>N7I</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/(Iso)eugenol_O-methyltransferase (Iso)eugenol O-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.146 2.1.1.146] </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=3tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tky OCA], [https://pdbe.org/3tky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tky RCSB], [https://www.ebi.ac.uk/pdbsum/3tky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tky ProSAT]</span></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=3tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tky OCA], [https://pdbe.org/3tky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tky RCSB], [https://www.ebi.ac.uk/pdbsum/3tky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tky ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/IEMT_CLABR IEMT_CLABR]] Catalyzes the methylation of the para-4-hydroxyl of both eugenol and (iso)eugenol to methyleugenol and isomethyleugenol, respectively. The resulting products are part of a complex mixture of low-molecular-weight volatile compounds emitted by the flowers to attract pollinators.
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[https://www.uniprot.org/uniprot/IEMT_CLABR IEMT_CLABR] Catalyzes the methylation of the para-4-hydroxyl of both eugenol and (iso)eugenol to methyleugenol and isomethyleugenol, respectively. The resulting products are part of a complex mixture of low-molecular-weight volatile compounds emitted by the flowers to attract pollinators.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Although the practice of protein engineering is industrially fruitful in creating biocatalysts and therapeutic proteins, applications of analogous techniques in the field of plant metabolic engineering are still in their infancy. Lignins are aromatic natural polymers derived from the oxidative polymerization of primarily three different hydroxycinnamyl alcohols, the monolignols. Polymerization of lignin starts with the oxidation of monolignols, followed by endwise cross-coupling of (radicals of) a monolignol and the growing oligomer/polymer. The para-hydroxyl of each monolignol is crucial for radical generation and subsequent coupling. Here, we describe the structure-function analysis and catalytic improvement of an artificial monolignol 4-O-methyltransferase created by iterative saturation mutagenesis and its use in modulating lignin and phenylpropanoid biosynthesis. We show that expressing the created enzyme in planta, thus etherifying the para-hydroxyls of lignin monomeric precursors, denies the derived monolignols any participation in the subsequent coupling process, substantially reducing lignification and, ultimately, lignin content. Concomitantly, the transgenic plants accumulated de novo synthesized 4-O-methylated soluble phenolics and wall-bound esters. The lower lignin levels of transgenic plants resulted in higher saccharification yields. Our study, through a structure-based protein engineering approach, offers a novel strategy for modulating phenylpropanoid/lignin biosynthesis to improve cell wall digestibility and diversify the repertories of biologically active compounds.
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An engineered monolignol 4-o-methyltransferase depresses lignin biosynthesis and confers novel metabolic capability in Arabidopsis.,Zhang K, Bhuiya MW, Pazo JR, Miao Y, Kim H, Ralph J, Liu CJ Plant Cell. 2012 Jul;24(7):3135-52. Epub 2012 Jul 31. PMID:22851762<ref>PMID:22851762</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 3tky" 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: Clabr]]
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[[Category: Clarkia breweri]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhuiya, M W]]
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[[Category: Bhuiya MW]]
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[[Category: Liu, C J]]
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[[Category: Liu CJ]]
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[[Category: Directed evolution]]
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[[Category: Regioselectivity]]
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[[Category: Saturation mutagenesis]]
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[[Category: Transferase]]
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Current revision

Monolignol o-methyltransferase (momt)

PDB ID 3tky

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OCA

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