5O7Y

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

5O7Y の概要

• エントリーDOI: 10.2210/pdb5o7y/pdb
• 分子名称: Thebaine 6-O-demethylase, NICKEL (II) ION, SUCCINIC ACID, ... (6 entities in total)
• 機能のキーワード: 2-oxoglutarate dependent dioxygenase, morphine biosynthesis, oripavine, thebaine, oxidoreductase
• 由来する生物種: Papaver somniferum (Opium poppy)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42381.04

構造登録者

Kluza, A.,Niedzialkowska, E.,Kurpiewska, K.,Porebski, P.J.,Borowski, T. (登録日: 2017-06-10, 公開日: 2018-02-14, 最終更新日: 2024-01-17)

主引用文献

Kluza, A.,Niedzialkowska, E.,Kurpiewska, K.,Wojdyla, Z.,Quesne, M.,Kot, E.,Porebski, P.J.,Borowski, T.
Crystal structure of thebaine 6-O-demethylase from the morphine biosynthesis pathway.
J. Struct. Biol., 202:229-235, 2018

PubMed Abstract: 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.

PubMed: 29408320
DOI: 10.1016/j.jsb.2018.01.007

実験手法

X-RAY DIFFRACTION (1.97 Å)