3c3y

<table><tr><td colspan='2'>[[3c3y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_ice_plant Common ice plant]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3C3Y FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caffeoyl-CoA_O-methyltransferase Caffeoyl-CoA O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.104 2.1.1.104] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3c3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c3y OCA], [http://pdbe.org/3c3y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c3y RCSB], [http://www.ebi.ac.uk/pdbsum/3c3y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c3y ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Plant S-adenosyl-l-methionine-dependent class I natural product O-methyltransferases (OMTs), related to animal catechol OMTs, are dependent on bivalent cations and strictly specific for the meta position of aromatic vicinal dihydroxy groups. While the primary activity of these class I enzymes is methylation of caffeoyl coenzyme A OMTs, a distinct subset is able to methylate a wider range of substrates, characterized by the promiscuous phenylpropanoid and flavonoid OMT. The observed broad substrate specificity resides in two regions: the N-terminus and a variable insertion loop near the C-terminus, which displays the lowest degree of sequence conservation between the two subfamilies. Structural and biochemical data, based on site-directed mutagenesis and domain exchange between the two enzyme types, present evidence that only small topological changes among otherwise highly conserved 3-D structures are sufficient to differentiate between an enzymatic generalist and an enzymatic specialist in plant natural product methylation.

Biochemical and structural analysis of substrate promiscuity in plant Mg2+-dependent O-methyltransferases.,Kopycki JG, Rauh D, Chumanevich AA, Neumann P, Vogt T, Stubbs MT J Mol Biol. 2008 Apr 18;378(1):154-64. Epub 2008 Feb 20. PMID:18342334<ref>PMID:18342334</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Caffeoyl-CoA O-methyltransferase]]

[[Category: Common ice plant]]

[[Category: Kopycki, J G]]

[[Category: Neumann, P]]

[[Category: Rauh, D]]

[[Category: Stubbs, M T]]

[[Category: O-methyltransferase]]

[[Category: Transferase]]