4ems
From Proteopedia
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| - | + | ==Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum== | |
| - | + | <StructureSection load='4ems' size='340' side='right' caption='[[4ems]], [[Resolution|resolution]] 1.75Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <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> | ||
| + | </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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e70|4e70]]</td></tr> | ||
| + | <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> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4ems RCSB], [http://www.ebi.ac.uk/pdbsum/4ems PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Linum nodiflorum]] | [[Category: Linum nodiflorum]] | ||
| - | [[Category: Heine, A | + | [[Category: Heine, A]] |
| - | [[Category: Petersen, M | + | [[Category: Petersen, M]] |
| - | [[Category: Wolters, S | + | [[Category: Wolters, S]] |
[[Category: Coniferyl alcohol]] | [[Category: Coniferyl alcohol]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
Revision as of 04:48, 27 January 2015
Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum
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