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3ale
From Proteopedia
(Difference between revisions)
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| - | + | ==A type III polyketide synthase that produces diarylheptanoid== | |
| - | + | <StructureSection load='3ale' size='340' side='right' caption='[[3ale]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3ale]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ALE FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cgk|1cgk]], [[1u0u|1u0u]], [[3a5q|3a5q]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OJ1001_C01.122, OSJNBb0002J01.6, Os07g0271500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ale OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ale RCSB], [http://www.ebi.ac.uk/pdbsum/3ale PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://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> | [[http://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;"> | ||
| + | == 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<ref>PMID:21041675</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Japanese rice]] | [[Category: Japanese rice]] | ||
| - | [[Category: Abe, I | + | [[Category: Abe, I]] |
| - | [[Category: Kato, R | + | [[Category: Kato, R]] |
| - | [[Category: Morita, H | + | [[Category: Morita, H]] |
| - | [[Category: Sugio, S | + | [[Category: Sugio, S]] |
[[Category: Benzalacetone synthase]] | [[Category: Benzalacetone synthase]] | ||
[[Category: Diarylheptanoid]] | [[Category: Diarylheptanoid]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Type iii polyketide synthase]] | [[Category: Type iii polyketide synthase]] | ||
Revision as of 11:59, 25 December 2014
A type III polyketide synthase that produces diarylheptanoid
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