5cxo

Intriguing role of epoxide hydrolase/cyclase-like enzyme SalBIII in pyran ring formation in polyether salinomycin

spinqualitylabelsall models 5cxo, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cxo is a 2 chain structure with sequence from Streptomyces albus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: P6G Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H6D578_STRA4 Publication Abstract from PubMed Tetrahydropyran rings are a common feature of complex polyketide natural products, but much remains to be learned about the enzymology of their formation. The enzyme SalBIII from the salinomycin biosynthetic pathway resembles other polyether epoxide hydrolases/cyclases of the MonB family, but SalBIII plays no role in the conventional cascade of ring opening/closing. Mutation in the salBIII gene gave a metabolite in which ring A is not formed. Using this metabolite in vitro as a substrate analogue, SalBIII has been shown to form pyran ring A. We have determined the X-ray crystal structure of SalBIII, and structure-guided mutagenesis of putative active-site residues has identified Asp38 and Asp104 as an essential catalytic dyad. The demonstrated pyran synthase activity of SalBIII further extends the impressive catalytic versatility of alpha+beta barrel fold proteins. Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis.,Luhavaya H, Dias MV, Williams SR, Hong H, de Oliveira LG, Leadlay PF Angew Chem Int Ed Engl. 2015 Sep 17. doi: 10.1002/anie.201507090. PMID:26377145 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Epoxide hydrolase 3D structures

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