1u0u | pdb_00001u0u

An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: Pine stilbene synthase structure

spinqualitylabelsall models 1u0u, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1u0u is a 6 chain structure with sequence from Pinus sylvestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.11Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DPSS_PINSY 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 Stilbene synthase (STS) and chalcone synthase (CHS) each catalyze the formation of a tetraketide intermediate from a CoA-tethered phenylpropanoid starter and three molecules of malonyl-CoA, but use different cyclization mechanisms to produce distinct chemical scaffolds for a variety of plant natural products. Here we present the first STS crystal structure and identify, by mutagenic conversion of alfalfa CHS into a functional stilbene synthase, the structural basis for the evolution of STS cyclization specificity in type III polyketide synthase (PKS) enzymes. Additional mutagenesis and enzymatic characterization confirms that electronic effects rather than steric factors balance competing cyclization specificities in CHS and STS. Finally, we discuss the problematic in vitro reconstitution of plant stilbenecarboxylate pathways, using insights from existing biomimetic polyketide cyclization studies to generate a novel mechanistic hypothesis to explain stilbenecarboxylate biosynthesis. An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases.,Austin MB, Bowman ME, Ferrer JL, Schroder J, Noel JP Chem Biol. 2004 Sep;11(9):1179-94. PMID:15380179 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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