6AIO

Crystal structure of p-nitrophenol 4-monooxygenase PnpA from Pseudomonas putida DLL-E4

6AIO の概要

• エントリーDOI: 10.2210/pdb6aio/pdb
• 分子名称: PnpA (2 entities in total)
• 機能のキーワード: p-nitrophenol 4-monooxygenase, flavoprotein
• 由来する生物種: Pseudomonas putida (Arthrobacter siderocapsulatus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93256.09

構造登録者

Chen, Q.Z.,Huang, Y.,Duan, Y.J.,Li, Z.K.,Liu, W.D.,Cui, Z.L. (登録日: 2018-08-24, 公開日: 2018-10-31, 最終更新日: 2023-11-22)

主引用文献

Chen, Q.Z.,Huang, Y.,Duan, Y.J.,Li, Z.K.,Cui, Z.L.,Liu, W.D.
Crystal structure of p-nitrophenol 4-monooxygenase PnpA from Pseudomonas putida DLL-E4: The key enzyme involved in p-nitrophenol degradation.
Biochem. Biophys. Res. Commun., 504:715-720, 2018

PubMed Abstract: p-Nitrophenol 4-monooxygenase PnpA, the key enzyme in the hydroquinone pathway of p-nitrophenol (PNP) degradation, catalyzes the monooxygenase reaction of PNP to p-benzoquinone in the presence of FAD and NADH. Here, we determined the first crystal structure of PnpA from Pseudomonas putida DLL-E4 in its apo and FAD-complex forms to a resolution of 2.04 Å and 2.48 Å, respectively. The PnpA structure shares a common fold with hydroxybenzoate hydroxylases, despite a low amino sequence identity of 14-18%, confirming it to be a member of the Class A flavoprotein monooxygenases. However, substrate docking studies of PnpA indicated that the residues stabilizing the substrate in an orientation suitable for catalysis are not observed in other homologous hydroxybenzoate hydroxylases, suggesting PnpA employs a unique catalytic mechanism. This work expands our understanding on the reaction mode for this enzyme class.

PubMed: 30217456
DOI: 10.1016/j.bbrc.2018.09.040

実験手法

X-RAY DIFFRACTION (2.04 Å)