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| | <StructureSection load='5uc5' size='340' side='right'caption='[[5uc5]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5uc5' size='340' side='right'caption='[[5uc5]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5uc5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UC5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uc5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Malus_domestica Malus domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UC5 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.102Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5uc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc5 OCA], [http://pdbe.org/5uc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uc5 RCSB], [http://www.ebi.ac.uk/pdbsum/5uc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc5 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=5uc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc5 OCA], [https://pdbe.org/5uc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uc5 RCSB], [https://www.ebi.ac.uk/pdbsum/5uc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/K9MUA0_MALDO K9MUA0_MALDO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5uc5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5uc5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chalcone synthase|Chalcone synthase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Naringenin-chalcone synthase]] | + | [[Category: Malus domestica]] |
| - | [[Category: Jr, C E.Stewart]]
| + | [[Category: Noel JP]] |
| - | [[Category: Noel, J P]] | + | [[Category: Stewart Jr CE]] |
| - | [[Category: Polyketide]] | + | |
| - | [[Category: Thiolase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
K9MUA0_MALDO
Publication Abstract from PubMed
Biphenyl synthase and benzophenone synthase constitute an evolutionarily distinct clade of type III polyketide synthases (PKSs) that use benzoic acid-derived substrates to produce defense metabolites in plants. The use of benzoyl-CoA as an endogenous substrate is unusual for type III PKSs. Moreover, sequence analyses indicate that the residues responsible for the functional diversification of type III PKSs are mutated in benzoic acid-specific type III PKSs. In order to gain a better understanding of structure-function relationships within the type III PKS family, the crystal structures of biphenyl synthase from Malus x domestica and benzophenone synthase from Hypericum androsaemum were compared with the structure of an archetypal type III PKS: chalcone synthase from Malus x domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions. Collectively, these results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants.
Molecular architectures of benzoic acid-specific type III polyketide synthases.,Stewart C Jr, Woods K, Macias G, Allan AC, Hellens RP, Noel JP Acta Crystallogr D Struct Biol. 2017 Dec 1;73(Pt 12):1007-1019. doi:, 10.1107/S2059798317016618. Epub 2017 Nov 30. PMID:29199980[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stewart C Jr, Woods K, Macias G, Allan AC, Hellens RP, Noel JP. Molecular architectures of benzoic acid-specific type III polyketide synthases. Acta Crystallogr D Struct Biol. 2017 Dec 1;73(Pt 12):1007-1019. doi:, 10.1107/S2059798317016618. Epub 2017 Nov 30. PMID:29199980 doi:http://dx.doi.org/10.1107/S2059798317016618
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