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4evi
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4evi]] 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=4EVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EVI FirstGlance]. <br> | <table><tr><td colspan='2'>[[4evi]] 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=4EVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EVI FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C9M:2-METHOXY-4-[(1E)-3-METHOXYPROP-1-EN-1-YL]PHENOL'>C9M</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.015Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C9M:2-METHOXY-4-[(1E)-3-METHOXYPROP-1-EN-1-YL]PHENOL'>C9M</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4evi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4evi OCA], [https://pdbe.org/4evi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4evi RCSB], [https://www.ebi.ac.uk/pdbsum/4evi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4evi 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=4evi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4evi OCA], [https://pdbe.org/4evi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4evi RCSB], [https://www.ebi.ac.uk/pdbsum/4evi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4evi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A6XNE6_9ROSI A6XNE6_9ROSI] | [https://www.uniprot.org/uniprot/A6XNE6_9ROSI A6XNE6_9ROSI] | ||
| - | <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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4evi" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum in Complex with Coniferyl Alcohol 9-Methyl Ether and S -Adenosyl-L-Homocysteine
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