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| | <StructureSection load='3ale' size='340' side='right'caption='[[3ale]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3ale' size='340' side='right'caption='[[3ale]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ale]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ALE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ale]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ALE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cgk|1cgk]], [[1u0u|1u0u]], [[3a5q|3a5q]]</div></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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OJ1001_C01.122, OSJNBb0002J01.6, Os07g0271500 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</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=3ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ale OCA], [https://pdbe.org/3ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ale RCSB], [https://www.ebi.ac.uk/pdbsum/3ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ale 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=3ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ale OCA], [https://pdbe.org/3ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ale RCSB], [https://www.ebi.ac.uk/pdbsum/3ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ale ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CUS_ORYSJ CUS_ORYSJ]] Plant-specific type III polyketide synthase (PKS) that catalyzes the one-pot formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA.<ref>PMID:21041675</ref>
| + | [https://www.uniprot.org/uniprot/CUS_ORYSJ CUS_ORYSJ] Plant-specific type III polyketide synthase (PKS) that catalyzes the one-pot formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA.<ref>PMID:21041675</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Japanese rice]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abe, I]] | + | [[Category: Oryza sativa Japonica Group]] |
| - | [[Category: Kato, R]] | + | [[Category: Abe I]] |
| - | [[Category: Morita, H]] | + | [[Category: Kato R]] |
| - | [[Category: Sugio, S]] | + | [[Category: Morita H]] |
| - | [[Category: Benzalacetone synthase]]
| + | [[Category: Sugio S]] |
| - | [[Category: Diarylheptanoid]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Type iii polyketide synthase]]
| + | |
| Structural highlights
Function
CUS_ORYSJ Plant-specific type III polyketide synthase (PKS) that catalyzes the one-pot formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA.[1]
Publication Abstract from PubMed
Curcuminoid synthase (CUS) from Oryza sativa is a plant-specific type III polyketide synthase (PKS) that catalyzes the remarkable one-pot formation of the C(6)-C(7)-C(6) diarylheptanoid scaffold of bisdemethoxycurcumin, by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA. The crystal structure of O. sativa CUS was solved at 2.5-A resolution, which revealed a unique, downward expanding active-site architecture, previously unidentified in the known type III PKSs. The large active-site cavity is long enough to accommodate the two C(6)-C(3) coumaroyl units and one malonyl unit. Furthermore, the crystal structure indicated the presence of a putative nucleophilic water molecule, which forms hydrogen bond networks with Ser351-Asn142-H(2)O-Tyr207-Glu202, neighboring the catalytic Cys174 at the active-site center. These observations suggest that CUS employs unique catalytic machinery for the one-pot formation of the C(6)-C(7)-C(6) scaffold. Thus, CUS utilizes the nucleophilic water to terminate the initial polyketide chain elongation at the diketide stage. Thioester bond cleavage of the enzyme-bound intermediate generates 4-coumaroyldiketide acid, which is then kept within the downward expanding pocket for subsequent decarboxylative condensation with the second 4-coumaroyl-CoA starter, to produce bisdemethoxycurcumin. The structure-based site-directed mutants, M265L and G274F, altered the substrate and product specificities to accept 4-hydroxyphenylpropionyl-CoA as the starter to produce tetrahydrobisdemethoxycurcumin. These findings not only provide a structural basis for the catalytic machinery of CUS but also suggest further strategies toward expanding the biosynthetic repertoire of the type III PKS enzymes.
Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa.,Morita H, Wanibuchi K, Nii H, Kato R, Sugio S, Abe I Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19778-83. Epub 2010 Nov 1. PMID:21041675[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morita H, Wanibuchi K, Nii H, Kato R, Sugio S, Abe I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19778-83. Epub 2010 Nov 1. PMID:21041675 doi:http://dx.doi.org/10.1073/pnas.1011499107
- ↑ Morita H, Wanibuchi K, Nii H, Kato R, Sugio S, Abe I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19778-83. Epub 2010 Nov 1. PMID:21041675 doi:http://dx.doi.org/10.1073/pnas.1011499107
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