3c3y: Difference between revisions

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{{Seed}}
[[Image:3c3y.png|left|200px]]


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==Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum==
The line below this paragraph, containing "STRUCTURE_3c3y", creates the "Structure Box" on the page.
<StructureSection load='3c3y' size='340' side='right'caption='[[3c3y]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3c3y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesembryanthemum_crystallinum Mesembryanthemum crystallinum]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3C3Y FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.371&#8491;</td></tr>
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<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>
{{STRUCTURE_3c3y|  PDB=3c3y  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c3y OCA], [https://pdbe.org/3c3y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c3y RCSB], [https://www.ebi.ac.uk/pdbsum/3c3y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c3y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6YI95_MESCR Q6YI95_MESCR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/3c3y_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3c3y ConSurf].
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<div style="background-color:#fffaf0;">
== 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.


===Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum===
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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<div class="pdbe-citations 3c3y" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18342334 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18342334}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3C3Y is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mesembryanthemum_crystallinum Mesembryanthemum crystallinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C3Y OCA].
 
==Reference==
<ref group="xtra">PMID:18342334</ref><references group="xtra"/>
[[Category: Caffeoyl-CoA O-methyltransferase]]
[[Category: Mesembryanthemum crystallinum]]
[[Category: Mesembryanthemum crystallinum]]
[[Category: Kopycki, J G.]]
[[Category: Kopycki JG]]
[[Category: Neumann, P.]]
[[Category: Neumann P]]
[[Category: Rauh, D.]]
[[Category: Rauh D]]
[[Category: Stubbs, M T.]]
[[Category: Stubbs MT]]
[[Category: O-methyltransferase]]
[[Category: Plant secondary metabolism]]
 
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