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==Crystal Structure of sorghum caffeoyl-CoA O-methyltransferase (CCoAOMT)==
==Crystal Structure of sorghum caffeoyl-CoA O-methyltransferase (CCoAOMT)==
<StructureSection load='5kva' size='340' side='right' caption='[[5kva]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='5kva' size='340' side='right'caption='[[5kva]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5kva]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KVA FirstGlance]. <br>
<table><tr><td colspan='2'>[[5kva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorghum_bicolor Sorghum bicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KVA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 1.827&#8491;</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=5kva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kva OCA], [http://pdbe.org/5kva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kva RCSB], [http://www.ebi.ac.uk/pdbsum/5kva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kva ProSAT]</span></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=SAM:S-ADENOSYLMETHIONINE'>SAM</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=5kva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kva OCA], [https://pdbe.org/5kva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kva RCSB], [https://www.ebi.ac.uk/pdbsum/5kva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kva ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/C5Z4W3_SORBI C5Z4W3_SORBI]
Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) is an S-adenosyl methionine (SAM)-dependent O-methyltransferase responsible for methylation of the meta-hydroxyl group of caffeoyl-CoA, on the pathway to monolignols with their ring methoxylation status characteristic of guaiacyl or syringyl units in lignin. In order to better understand the unique class of type-2 O-methyltransferases from monocots, we have characterized CCoAOMT from sorghum (Sorghum bicolor) (SbCCoAOMT), including the SAM binary complex crystal structure, steady state enzyme kinetics, isothermal titration calorimetry (ITC), inductively coupled plasma-optical emission spectroscopy (ICP-OES) and molecular docking. Key amino acid residues were validated with site-directed mutagenesis. ITC data indicated a sequential binding mechanism for SbCCoAOMT, wherein SAM binds prior to caffeoyl-CoA, and the enzyme showed allosteric behavior with respect to it. 5-Hydroxyferuloyl-CoA was not a substrate for SbCCoAOMT. We propose a catalytic mechanism in which Lys180 acts as a catalytic base and deprotonates the reactive hydroxyl group of caffeoyl-CoA. This deprotonation is facilitated by the coordination of the reactive hydroxyl group by Ca2+ in the active site, lowering the pKa of the 3'-OH group. Collectively, these data give a new perspective on the catalytic mechanism of CCoAOMTs and provide a basis for the functional diversity exhibited by type-2 plant OMTs that contain a unique insertion loop (residues 208-231) conferring affinity for phenylpropanoid-CoA thioesters.
 
Determination of the structure and catalytic mechanism of Sorghum bicolor caffeoyl-CoA O-methyltransferase.,Walker AM, Sattler SA, Regner MR, Jones JP, Ralph J, Vermerris W, Sattler SE, Kang C Plant Physiol. 2016 Jul 25. pii: pp.00845.2016. PMID:27457122<ref>PMID:27457122</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kva" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Jones, J P]]
[[Category: Large Structures]]
[[Category: Kang, C]]
[[Category: Sorghum bicolor]]
[[Category: Ralph, J]]
[[Category: Jones JP]]
[[Category: Regner, M]]
[[Category: Kang C]]
[[Category: Sattler, S A]]
[[Category: Ralph J]]
[[Category: Sattler, S E]]
[[Category: Regner M]]
[[Category: Vermerris, W]]
[[Category: Sattler SA]]
[[Category: Walker, A M]]
[[Category: Sattler SE]]
[[Category: Caffeoyl-coa o-methyltransferase]]
[[Category: Vermerris W]]
[[Category: Ccoaomt]]
[[Category: Walker AM]]
[[Category: Ccomt omt]]
[[Category: Coenzyme some]]
[[Category: Methyltransferase]]
[[Category: Sam o-methyltransferase]]
[[Category: Sbccoaomt]]
[[Category: Transferase]]
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