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| ==CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED ISOFLAVONE O-METHYLTRANSFERASE==
| | #REDIRECT [[6cig]] This PDB entry is obsolete and replaced by 6cig |
| <StructureSection load='1fpx' size='340' side='right' caption='[[1fpx]], [[Resolution|resolution]] 1.65Å' scene=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[1fpx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FPX FirstGlance]. <br>
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| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fp1|1fp1]], [[1fp2|1fp2]], [[1fpq|1fpq]]</td></tr>
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| <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=1fpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fpx RCSB], [http://www.ebi.ac.uk/pdbsum/1fpx PDBsum]</span></td></tr>
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| </table>
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| == Evolutionary Conservation ==
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| [[Image:Consurf_key_small.gif|200px|right]]
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| Check<jmol>
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| <jmolCheckbox>
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| <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpx_consurf.spt"</scriptWhenChecked>
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| <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| <text>to colour the structure by Evolutionary Conservation</text>
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| </jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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| <div style="clear:both"></div>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Chalcone O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.
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| Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.,Zubieta C, He XZ, Dixon RA, Noel JP Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575<ref>PMID:11224575</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| == References ==
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| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Medicago sativa]]
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| [[Category: Dixon, R A]]
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| [[Category: Noel, J P]]
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| [[Category: Zubieta, C]]
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| [[Category: S-adenosymethionine complex]]
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| [[Category: Selenomethionine]]
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| [[Category: Transferase]]
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