7dls | pdb_00007dls

Cytochrome P450 (CYP105D18) complex with papaverine

spinqualitylabelsall models 7dls, resolution 2.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7dls is a 1 chain structure with sequence from Streptomyces laurentii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.06Å Ligands: EV1, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A160P685_STRLU Publication Abstract from PubMed The bacterial CYP105 family is involved in secondary metabolite biosynthetic pathways and plays essential roles in the biotransformation of xenobiotics. This study investigates the newly identified H2O2-mediated CYP105D18 from Streptomyces laurentii as the first bacterial CYP for N-oxidation. The catalytic efficiency of CYP105D18 for papaverine N-oxidation was 1.43 s(-1) microM (-1). The heme oxidation rate (k) was low (<0.3 min(-1)) in the presence of 200 mM H2O2. This high H2O2 tolerance capacity of CYP105D18 led to higher turnover prior to heme oxidation. Additionally, the high-resolution papaverine complexed structure and substrate-free structure of CYP105D18 were determined. Structural analysis and activity assay results revealed that CYP105D18 had a strong substrate preference for papaverine because of its bendable structure. These findings establish a basis for biotechnological applications of CYP105D18 in the pharmaceutical and medicinal industries. Characterization of high-H2O2-tolerant bacterial cytochrome P450 CYP105D18: insights into papaverine N-oxidation.,Pardhe BD, Do H, Jeong CS, Kim KH, Lee JH, Oh TJ IUCrJ. 2021 Jun 29;8(Pt 4):684-694. doi: 10.1107/S2052252521005522. eCollection, 2021 Jul 1. PMID:34258016 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 hydroxylase 3D structures

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