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1fpq

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[[Image:1fpq.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE==
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|PDB= 1fpq |SIZE=350|CAPTION= <scene name='initialview01'>1fpq</scene>, resolution 2.00&Aring;
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<StructureSection load='1fpq' size='340' side='right'caption='[[1fpq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>
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<table><tr><td colspan='2'>[[1fpq]] is a 1 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=1FPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPQ FirstGlance]. <br>
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|ACTIVITY=
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</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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpq OCA], [https://pdbe.org/1fpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpq RCSB], [https://www.ebi.ac.uk/pdbsum/1fpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpq ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1fp1|1FP1]], [[1fp2|1FP2]], [[1fpx|1FPX]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpq OCA], [http://www.ebi.ac.uk/pdbsum/1fpq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CHOMT_MEDSA CHOMT_MEDSA] Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.<ref>PMID:1731632</ref> <ref>PMID:9055445</ref>
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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpq_consurf.spt"</scriptWhenChecked>
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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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<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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==About this Structure==
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</jmolCheckbox>
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1FPQ is a [[Single protein]] structure of 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=1FPQ OCA].
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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=1fpq ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11224575 11224575]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Medicago sativa]]
[[Category: Medicago sativa]]
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[[Category: Single protein]]
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[[Category: Dixon RA]]
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[[Category: Dixon, R A.]]
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[[Category: Noel JP]]
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[[Category: Noel, J P.]]
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[[Category: Zubieta C]]
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[[Category: Zubieta, C.]]
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[[Category: selenomethionine substituted protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:47 2008''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

PDB ID 1fpq

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