3a5r

Benzalacetone synthase from Rheum palmatum complexed with 4-coumaroyl-primed monoketide intermediate

spinqualitylabelsall models 3a5r, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3a5r is a 2 chain structure with sequence from Rheum palmatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: HC4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BAS_RHEPA Polyketide synthase producing 4-hydroxybenzalacetone. Can use p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Benzalacetone synthase (BAS), a plant-specific type III polyketide synthase (PKS), catalyzes a one-step decarboxylative condensation of malonyl-CoA and 4-coumaroyl-CoA to produce the diketide benzalacetone. We solved the crystal structures of both the wild-type and chalcone-producing I207L/L208F mutant of Rheum palmatum BAS at 1.8 A resolution. In addition, we solved the crystal structure of the wild-type enzyme, in which a monoketide coumarate intermediate is covalently bound to the catalytic cysteine residue, at 1.6 A resolution. This is the first direct evidence that type III PKS utilizes the cysteine as the nucleophile and as the attachment site for the polyketide intermediate. The crystal structures revealed that BAS utilizes an alternative, novel active-site pocket for locking the aromatic moiety of the coumarate, instead of the chalcone synthase's coumaroyl-binding pocket, which is lost in the active-site of the wild-type enzyme and restored in the I207L/L208F mutant. Furthermore, the crystal structures indicated the presence of a putative nucleophilic water molecule which forms hydrogen bond networks with the Cys-His-Asn catalytic triad. This suggested that BAS employs novel catalytic machinery for the thioester bond cleavage of the enzyme-bound diketide intermediate and the final decarboxylation reaction to produce benzalacetone. These findings provided a structural basis for the functional diversity of the type III PKS enzymes. A structure-based mechanism for benzalacetone synthase from Rheum palmatum.,Morita H, Shimokawa Y, Tanio M, Kato R, Noguchi H, Sugio S, Kohno T, Abe I Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):669-73. Epub 2009 Dec 18. PMID:20080733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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