3CHH

Crystal Structure of Di-iron AurF

3CHH の概要

• エントリーDOI: 10.2210/pdb3chh/pdb
• 関連するPDBエントリー: 3CHI
• 分子名称: p-Aminobenzoate N-Oxygenase, MU-OXO-DIIRON (3 entities in total)
• 機能のキーワード: di-iron oxygenase, oxidoreductase
• 由来する生物種: Streptomyces thioluteus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76514.32

構造登録者

Zhang, H.,Brunzelle, J.S.,Nair, S.K. (登録日: 2008-03-09, 公開日: 2008-05-27, 最終更新日: 2024-02-21)

主引用文献

Choi, Y.S.,Zhang, H.,Brunzelle, J.S.,Nair, S.K.,Zhao, H.
In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis.
Proc.Natl.Acad.Sci.Usa, 105:6858-6863, 2008

PubMed Abstract: p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme activity, the crystal structure of AurF in the oxidized state, and the cocrystal structure of AurF with its product pNBA. Our combined biochemical and structural analysis unequivocally indicates that AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates.

PubMed: 18458342
DOI: 10.1073/pnas.0712073105

実験手法

X-RAY DIFFRACTION (2 Å)