6kfw

The cytochrome P450 enzyme CxnD for C-S bond formation in chuangxinmycin biosynthesis

spinqualitylabelsall models 6kfw, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: D8L, HEM, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Microbial sulfur-containing secondary metabolites show various biological activities and the C-S bond-forming in their biosynthetic metabolism has not been thoroughly understood. Here, we present genetic, biochemical and structural characterization of a cytochrome P450 monooxygenase CxnD exhibiting C-S bond forming activity in S-heterocyclization of chuangxinmycin biosynthesis. In vivo and in vitro analyses demonstrated that CxnD generated an indole-fused dihydrothiopyran skeleton from a L-Trp-derived thiol intermediate. Furthermore, X-ray crystal structure of CxnD in complex with a substrate analogue and structure-based mutagenesis revealed intimate details of the substrate binding mode. A radical mechanism initiated by abstraction of the imino hydrogen atom or an electron from indole group of the substrate was proposed for CxnD, which provided valuable insights into the molecular basis for the intra-molecular C(sp2)-H thiolation by the P450 in chuangxinmycin biosynthesis. The cytochrome P450 catalyzing C-S bond formation in S-heterocyclization of chuangxinmycin biosynthesis.,Shi Y, Jiang Z, Hu X, Hu X, Gu R, Jiang B, Zuo L, Li X, Sun H, Zhang C, Wang L, Wu L, Hong B Angew Chem Int Ed Engl. 2021 Apr 21. doi: 10.1002/anie.202015814. PMID:33884733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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