2y3s | pdb_00002y3s

Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group

spinqualitylabelsall models 2y3s, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y3s is a 2 chain structure with sequence from Streptomyces sp. 307-9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: CL, FAD, GOL, MG, TIR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D3Y1I2_9ACTN Publication Abstract from PubMed Elucidation of natural product biosynthetic pathways provides important insights into the assembly of potent bioactive molecules, and expands access to unique enzymes able to selectively modify complex substrates. Here, we show full reconstitution, in vitro, of an unusual multi-step oxidative cascade for post-assembly-line tailoring of tirandamycin antibiotics. This pathway involves a remarkably versatile and iterative cytochrome P450 monooxygenase (TamI) and a flavin adenine dinucleotide-dependent oxidase (TamL), which act co-dependently through the repeated exchange of substrates. TamI hydroxylates tirandamycin C (TirC) to generate tirandamycin E (TirE), a previously unidentified tirandamycin intermediate. TirE is subsequently oxidized by TamL, giving rise to the ketone of tirandamycin D (TirD), after which a unique exchange back to TamI enables successive epoxidation and hydroxylation to afford, respectively, the final products tirandamycin A (TirA) and tirandamycin B (TirB). Ligand-free, substrate- and product-bound crystal structures of bicovalently flavinylated TamL oxidase reveal a likely mechanism for the C10 oxidation of TirE. Tirandamycin biosynthesis is mediated by co-dependent oxidative enzymes.,Carlson JC, Li S, Gunatilleke SS, Anzai Y, Burr DA, Podust LM, Sherman DH Nat Chem. 2011 Jul 17;3(8):628-33. doi: 10.1038/nchem.1087. PMID:21778983 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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