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<StructureSection load='1sus' size='340' side='right'caption='[[1sus]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1sus' size='340' side='right'caption='[[1sus]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sus]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SUS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sus]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUS 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>, <scene name='pdbligand=SPF:SINAPOYL+COENZYME+A'>SPF</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]] 2.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sui|1sui]]</div></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>, <scene name='pdbligand=SPF:SINAPOYL+COENZYME+A'>SPF</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCOMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Alfalfa])</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=1sus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sus OCA], [https://pdbe.org/1sus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sus RCSB], [https://www.ebi.ac.uk/pdbsum/1sus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sus ProSAT]</span></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=1sus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sus OCA], [http://pdbe.org/1sus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sus RCSB], [http://www.ebi.ac.uk/pdbsum/1sus PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sus ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CAMT_MEDSA CAMT_MEDSA]] Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.  
[https://www.uniprot.org/uniprot/CAMT_MEDSA CAMT_MEDSA] Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sus ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sus ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-l-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with the reaction products S-adenosine-l-homocysteine and feruloyl/sinapoyl CoAs presented here belong to a structurally and mechanistically distinct family of plant small molecule OMTs. These structures provide a new understanding of the substrate preferences and the catalytic mechanism accompanying CCoAOMT-mediated O-methylation of CoA-linked phenylpropanoid substrates.
Crystal structures of alfalfa caffeoyl coenzyme A 3-O-methyltransferase.,Ferrer JL, Zubieta C, Dixon RA, Noel JP Plant Physiol. 2005 Mar;137(3):1009-17. Epub 2005 Feb 25. PMID:15734921<ref>PMID:15734921</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sus" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alfalfa]]
[[Category: Caffeoyl-CoA O-methyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dixon, R A]]
[[Category: Medicago sativa]]
[[Category: Ferrer, J L]]
[[Category: Dixon RA]]
[[Category: Noel, J P]]
[[Category: Ferrer J-L]]
[[Category: Zubieta, C]]
[[Category: Noel JP]]
[[Category: O-methyltransferase]]
[[Category: Zubieta C]]
[[Category: Protein-cofactor-substrate complex]]
[[Category: Rossmann fold]]
[[Category: Transferase]]

Latest revision as of 08:34, 14 February 2024

Crystal structure of alfalfa feruoyl coenzyme A 3-O-methyltransferase

1sus, resolution 2.70Å

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