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2gas
From Proteopedia
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| - | [[Image:2gas.gif|left|200px]] | ||
| - | < | + | ==Crystal Structure of Isoflavone Reductase== |
| - | + | <StructureSection load='2gas' size='340' side='right'caption='[[2gas]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2gas]] is a 2 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=2GAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GAS FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=2gas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gas OCA], [https://pdbe.org/2gas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gas RCSB], [https://www.ebi.ac.uk/pdbsum/2gas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gas ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/IFR_MEDSA IFR_MEDSA] Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (-)-medicarpin, the major phytoalexin in Alfalfa. | |
| - | + | == 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/ga/2gas_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2gas ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Isoflavonoids play important roles in plant defense and exhibit a range of mammalian health-promoting activities. Isoflavone reductase (IFR) specifically recognizes isoflavones and catalyzes a stereospecific NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6A resolution. Structural analysis, molecular modeling and docking, and comparison with the structures of other NADPH-dependent enzymes, defined the putative binding sites for co-factor and substrate and potential key residues for enzyme activity and substrate specificity. Further mutagenesis has confirmed the role of Lys144 as a catalytic residue. This study provides a structural basis for understanding the enzymatic mechanism and substrate specificity of IFRs as well as the functions of IFR-like proteins. | Isoflavonoids play important roles in plant defense and exhibit a range of mammalian health-promoting activities. Isoflavone reductase (IFR) specifically recognizes isoflavones and catalyzes a stereospecific NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6A resolution. Structural analysis, molecular modeling and docking, and comparison with the structures of other NADPH-dependent enzymes, defined the putative binding sites for co-factor and substrate and potential key residues for enzyme activity and substrate specificity. Further mutagenesis has confirmed the role of Lys144 as a catalytic residue. This study provides a structural basis for understanding the enzymatic mechanism and substrate specificity of IFRs as well as the functions of IFR-like proteins. | ||
| - | + | Crystal structure of isoflavone reductase from alfalfa (Medicago sativa L.).,Wang X, He X, Lin J, Shao H, Chang Z, Dixon RA J Mol Biol. 2006 May 19;358(5):1341-52. Epub 2006 Mar 29. PMID:16600295<ref>PMID:16600295</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2gas" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Medicago sativa]] | [[Category: Medicago sativa]] | ||
| - | + | [[Category: Chang Z]] | |
| - | [[Category: Chang | + | [[Category: Dixon RA]] |
| - | [[Category: Dixon | + | [[Category: He X]] |
| - | [[Category: He | + | [[Category: Lin J]] |
| - | [[Category: Lin | + | [[Category: Shao H]] |
| - | [[Category: Shao | + | [[Category: Wang X]] |
| - | [[Category: Wang | + | |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Isoflavone Reductase
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Categories: Large Structures | Medicago sativa | Chang Z | Dixon RA | He X | Lin J | Shao H | Wang X
