5o7y | pdb_00005o7y

Thebaine 6-O-demethylase (T6ODM) from Papaver somniferum in complex with succinate

spinqualitylabelsall models 5o7y, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o7y is a 1 chain structure with sequence from Papaver somniferum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.97Å Ligands: EDO, NI, PEG, SIN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DIOX1_PAPSO Publication Abstract from PubMed Thebaine 6-O-demethylase (T6ODM) from Papaver somniferum (opium poppy), which belongs to the non-heme 2-oxoglutarate/Fe(II)-dependent dioxygenases (ODD) family, is a key enzyme in the morphine biosynthesis pathway. Initially, T6ODM was characterized as an enzyme catalyzing O-demethylation of thebaine to neopinone and oripavine to morphinone. However, the substrate range of T6ODM was recently expanded to a number of various benzylisoquinoline alkaloids. Here, we present crystal structures of T6ODM in complexes with 2-oxoglutarate (T6ODM:2OG, PDB: 5O9W) and succinate (T6ODM:SIN, PDB: 5O7Y). Both metal and 2OG binding sites display similarity to other proteins from the ODD family, but T6ODM is characterized by an exceptionally large substrate binding cavity, whose volume can partially explain the promiscuity of this enzyme. Moreover, the size of the cavity allows for binding of multiple molecules at once, posing a question about the substrate-driven specificity of the enzyme. Crystal structure of thebaine 6-O-demethylase from the morphine biosynthesis pathway.,Kluza A, Niedzialkowska E, Kurpiewska K, Wojdyla Z, Quesne M, Kot E, Porebski PJ, Borowski T J Struct Biol. 2018 Feb 8. pii: S1047-8477(18)30022-4. doi:, 10.1016/j.jsb.2018.01.007. PMID:29408320 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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