1d6f

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CHALCONE SYNTHASE C164A MUTANT

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-[[Image:1d6f.jpg|left|200px]]
- {{Structure
+==CHALCONE SYNTHASE C164A MUTANT==
-|PDB= 1d6f |SIZE=350|CAPTION= <scene name='initialview01'>1d6f</scene>, resolution 1.69&Aring;
+<StructureSection load='1d6f' size='340' side='right'caption='[[1d6f]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1d6f]] 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=1D6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D6F FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6f OCA], [https://pdbe.org/1d6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d6f RCSB], [https://www.ebi.ac.uk/pdbsum/1d6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d6f ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1bi5|1BI5]], [[1bq6|1BQ6]], [[1cgk|1CGK]], [[1cgz|1CGZ]], [[1chw|1CHW]], [[1cml|1CML]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6f OCA], [http://www.ebi.ac.uk/pdbsum/1d6f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6f RCSB]</span>
+== Function ==
-}}
+[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 ==
+[[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/d6/1d6f_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=1d6f ConSurf].
+<div style="clear:both"></div>
-'''CHALCONE SYNTHASE C164A MUTANT'''
+==See Also==
+*[[Chalcone synthase|Chalcone synthase]]
+== References ==
-==Overview==
+<references/>
-Chalcone synthase (CHS) catalyzes formation of the phenylpropanoid chalcone from one p-coumaroyl-CoA and three malonyl-coenzyme A (CoA) thioesters. The three-dimensional structure of CHS [Ferrer, J.-L., Jez, J. M., Bowman, M. E., Dixon, R. A., and Noel, J. P. (1999) Nat. Struct. Biol. 6, 775-784] suggests that four residues (Cys164, Phe215, His303, and Asn336) participate in the multiple decarboxylation and condensation reactions catalyzed by this enzyme. Here, we functionally characterize 16 point mutants of these residues for chalcone production, malonyl-CoA decarboxylation, and the ability to bind CoA and acetyl-CoA. Our results confirm Cys164's role as the active-site nucleophile in polyketide formation and elucidate the importance of His303 and Asn336 in the malonyl-CoA decarboxylation reaction. We suggest that Phe215 may help orient substrates at the active site during elongation of the polyketide intermediate. To better understand the structure-function relationships in some of these mutants, we also determined the crystal structures of the CHS C164A, H303Q, and N336A mutants refined to 1.69, 2.0, and 2.15 A resolution, respectively. The structure of the C164A mutant reveals that the proposed oxyanion hole formed by His303 and Asn336 remains undisturbed, allowing this mutant to catalyze malonyl-CoA decarboxylation without chalcone formation. The structures of the H303Q and N336A mutants support the importance of His303 and Asn336 in polarizing the thioester carbonyl of malonyl-CoA during the decarboxylation reaction. In addition, both of these residues may also participate in stabilizing the tetrahedral transition state during polyketide elongation. Conservation of the catalytic functions of the active-site residues may occur across a wide variety of condensing enzymes, including other polyketide and fatty acid synthases.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-D6F 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=1D6F OCA].
-==Reference==
-Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase., Jez JM, Ferrer JL, Bowman ME, Dixon RA, Noel JP, Biochemistry. 2000 Feb 8;39(5):890-902. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10653632 10653632]
 [[Category: Medicago sativa]]
-[[Category: Naringenin-chalcone synthase]]
+[[Category: Bowman ME]]
-[[Category: Single protein]]
+[[Category: Dixon RA]]
-[[Category: Bowman, M E.]]
+[[Category: Ferrer JL]]
-[[Category: Dixon, R A.]]
+[[Category: Jez JM]]
-[[Category: Ferrer, J L.]]
+[[Category: Noel JP]]
-[[Category: Jez, J M.]]
-[[Category: Noel, J P.]]
-[[Category: flavonoid biosynthesis]]
-[[Category: malonyl-coa decarboxylation]]
-[[Category: polypetide synthase]]
-[[Category: site- directed mutant]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:32 2008''

1d6f

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CHALCONE SYNTHASE C164A MUTANT

Structural highlights

Function

Evolutionary Conservation

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