1jwx

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<StructureSection load='1jwx' size='340' side='right'caption='[[1jwx]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
<StructureSection load='1jwx' size='340' side='right'caption='[[1jwx]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1jwx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1jwx]] 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=1JWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWX FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
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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]] 1.63&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bi5|1bi5]]</div></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=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHS2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Alfalfa])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span></td></tr>
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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=1jwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwx OCA], [https://pdbe.org/1jwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwx RCSB], [https://www.ebi.ac.uk/pdbsum/1jwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwx ProSAT]</span></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=1jwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwx OCA], [https://pdbe.org/1jwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwx RCSB], [https://www.ebi.ac.uk/pdbsum/1jwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CHS2_MEDSA CHS2_MEDSA]] The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.<ref>PMID:10653632</ref> <ref>PMID:11732902</ref> <ref>PMID:11959984</ref> <ref>PMID:15380179</ref>
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[https://www.uniprot.org/uniprot/CHS2_MEDSA CHS2_MEDSA] The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.<ref>PMID:10653632</ref> <ref>PMID:11732902</ref> <ref>PMID:11959984</ref> <ref>PMID:15380179</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1jwx ConSurf].
</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=1jwx ConSurf].
<div style="clear:both"></div>
<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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Type III polyketide synthases (PKS) generate an array of natural products by condensing multiple acetyl units derived from malonyl-CoA to thioester-linked starter molecules covalently bound in the PKS active site. One strategy adopted by Nature for increasing the functional diversity of these biosynthetic enzymes involves modifying polyketide assembly by altering the preference for starter molecules. Chalcone synthase (CHS) is a ubiquitous plant PKS and the first type III PKS described functionally and structurally. Guided by the three-dimensional structure of CHS, Phe-215 and Phe-265, which are situated at the active site entrance, were targeted for site-directed mutagenesis to diversify CHS activity. The resulting mutants were screened against a panel of aliphatic and aromatic CoA-linked starter molecules to evaluate the degree of starter molecule specificity in CHS. Although wild-type CHS accepts a number of natural CoA thioesters, it does not use N-methylanthraniloyl-CoA as a substrate. Substitution of Phe-215 by serine yields a CHS mutant that preferentially accepts this CoA-thioester substrate to generate a novel alkaloid, namely N-methylanthraniloyltriacetic acid lactone. These results demonstrate that a point mutation in CHS dramatically shifts the molecular selectivity of this enzyme. This structure-based approach to metabolic redesign represents an initial step toward tailoring the biosynthetic activity of plant type III PKS.
 
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Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity.,Jez JM, Bowman ME, Noel JP Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5319-24. PMID:11959984<ref>PMID:11959984</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1jwx" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alfalfa]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Naringenin-chalcone synthase]]
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[[Category: Medicago sativa]]
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[[Category: Bowman, M E]]
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[[Category: Bowman ME]]
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[[Category: Jez, J M]]
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[[Category: Jez JM]]
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[[Category: Noel, J P]]
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[[Category: Noel JP]]
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[[Category: Altered substrate specificity]]
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[[Category: Ketoacyl synthase]]
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[[Category: Polyketide synthase]]
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[[Category: Transferase]]
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Current revision

Chalcone Synthase--F215S mutant

PDB ID 1jwx

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