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4ems

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==Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum==
==Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum==
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<StructureSection load='4ems' size='340' side='right' caption='[[4ems]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='4ems' size='340' side='right'caption='[[4ems]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ems]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Linum_nodiflorum Linum nodiflorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EMS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ems]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Linum_nodiflorum Linum nodiflorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EMS 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=GOL:GLYCEROL'>GOL</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]] 1.7534&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e70|4e70]]</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=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA9OMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=407264 Linum nodiflorum])</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=4ems FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ems OCA], [https://pdbe.org/4ems PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ems RCSB], [https://www.ebi.ac.uk/pdbsum/4ems PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ems 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=4ems FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ems OCA], [http://pdbe.org/4ems PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ems RCSB], [http://www.ebi.ac.uk/pdbsum/4ems PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ems ProSAT]</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/A6XNE6_9ROSI A6XNE6_9ROSI]
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Coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum (Linaceae) catalyzes the unusual methylation of the side-chain hydroxyl group of coniferyl alcohol. The protein was heterologously expressed in Escherichia coli as a hexahistidine derivative and purified for crystallization. Diffracting crystals were obtained of the pure protein and of its selenomethionine derivative, as well as of complexes with coniferyl alcohol and with S-adenosyl-L-homocysteine together with coniferyl alcohol 9-O-methyl ether (PDB entries 4ems, 4e70 and 4evi, respectively). The X-ray structures show that the phenylpropanoid binding mode differs from other phenylpropanoid O-methyltransferases such as caffeic acid O-methyltransferase. Moreover, the active site lacks the usually conserved and catalytic histidine residue and thus implies a different reaction mode for methylation. Site-directed mutagenesis was carried out to identify critical amino acids. The binding order of coniferyl alcohol and S-adenosyl-L-methionine was investigated by isothermal titration calorimetry experiments.
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Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.,Wolters S, Neeb M, Berim A, Schulze Wischeler J, Petersen M, Heine A Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):888-900. doi:, 10.1107/S0907444913002874. Epub 2013 Apr 19. PMID:23633600<ref>PMID:23633600</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 4ems" 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: Large Structures]]
[[Category: Linum nodiflorum]]
[[Category: Linum nodiflorum]]
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[[Category: Heine, A]]
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[[Category: Heine A]]
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[[Category: Petersen, M]]
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[[Category: Petersen M]]
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[[Category: Wolters, S]]
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[[Category: Wolters S]]
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[[Category: Coniferyl alcohol]]
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[[Category: Dimer]]
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[[Category: Methylation]]
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[[Category: Phenylpropanoid]]
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[[Category: Rossmann fold]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Small molecule o-methyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum

PDB ID 4ems

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