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1zg3

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(New page: 200px<br /><applet load="1zg3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zg3, resolution 2.35&Aring;" /> '''Crystal structure of...)
Current revision (09:04, 14 February 2024) (edit) (undo)
 
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[[Image:1zg3.gif|left|200px]]<br /><applet load="1zg3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zg3, resolution 2.35&Aring;" />
 
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'''Crystal structure of the isoflavanone 4'-O-methyltransferase complexed with SAH and 2,7,4'-trihydroxyisoflavanone'''<br />
 
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==Overview==
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==Crystal structure of the isoflavanone 4'-O-methyltransferase complexed with SAH and 2,7,4'-trihydroxyisoflavanone==
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In leguminous plants such as pea (Pisum sativum), alfalfa (Medicago, sativa), barrel medic (Medicago truncatula), and chickpea (Cicer, arietinum), 4'-O-methylation of isoflavonoid natural products occurs early, in the biosynthesis of defense chemicals known as phytoalexins. However, among these four species, only pea catalyzes 3-O-methylation that converts, the pterocarpanoid isoflavonoid 6a-hydroxymaackiain to pisatin. In pea, pisatin is important for chemical resistance to the pathogenic fungus, Nectria hematococca. While barrel medic does not biosynthesize, 6a-hydroxymaackiain, when cell suspension cultures are fed, 6a-hydroxymaackiain, they accumulate pisatin. In vitro, hydroxyisoflavanone 4'-O-methyltransferase (HI4'OMT) from barrel medic, exhibits nearly identical steady state kinetic parameters for the, 4'-O-methylation of the isoflavonoid intermediate, 2,7,4'-trihydroxyisoflavanone and for the 3-O-methylation of the, 6a-hydroxymaackiain isoflavonoid-derived pterocarpanoid intermediate found, in pea. Protein x-ray crystal structures of HI4'OMT substrate complexes, revealed identically bound conformations for the 2S,3R-stereoisomer of, 2,7,4'-trihydroxyisoflavanone and the 6aR,11aR-stereoisomer of, 6a-hydroxymaackiain. These results suggest how similar conformations, intrinsic to seemingly distinct chemical substrates allowed leguminous, plants to use homologous enzymes for two different biosynthetic reactions., The three-dimensional similarity of natural small molecules represents one, explanation for how plants may rapidly recruit enzymes for new, biosynthetic reactions in response to changing physiological and, ecological pressures.
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<StructureSection load='1zg3' size='340' side='right'caption='[[1zg3]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1zg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZG3 FirstGlance]. <br>
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1ZG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula] with 2HI and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZG3 OCA].
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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]] 2.35&#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=2HI:(2S,3R)-2,7-DIHYDROXY-3-(4-HYDROXYPHENYL)-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>2HI</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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==Reference==
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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=1zg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zg3 OCA], [https://pdbe.org/1zg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1zg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zg3 ProSAT]</span></td></tr>
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Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses., Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP, Plant Cell. 2006 Dec;18(12):3656-69. Epub 2006 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17172354 17172354]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/I4OMT_MEDTR I4OMT_MEDTR]
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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/zg/1zg3_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/main_output.php?pdb_ID=1zg3 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Medicago truncatula]]
[[Category: Medicago truncatula]]
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[[Category: Single protein]]
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[[Category: Deavours BE]]
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[[Category: Deavours, B.E.]]
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[[Category: Dixon RA]]
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[[Category: Dixon, R.A.]]
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[[Category: Ferrer J-L]]
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[[Category: Ferrer, J.L.]]
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[[Category: Liu C-J]]
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[[Category: Liu, C.J.]]
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[[Category: Noel JP]]
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[[Category: Noel, J.P.]]
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[[Category: Richard S]]
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[[Category: Richard, S.]]
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[[Category: 2HI]]
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[[Category: SAH]]
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[[Category: isoflavanone 4'-o-methyltransferase]]
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[[Category: rossman fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:52:25 2007''
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Current revision

Crystal structure of the isoflavanone 4'-O-methyltransferase complexed with SAH and 2,7,4'-trihydroxyisoflavanone

PDB ID 1zg3

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