3CHU

Crystal Structure of Di-iron Aurf

Summary for 3CHU

• Entry DOI: 10.2210/pdb3chu/pdb
• Related: 3CHH 3CHI 3CHT
• Descriptor: p-Aminobenzoate N-Oxygenase, MU-OXO-DIIRON (3 entities in total)
• Functional Keywords: di-iron oxygenase, oxidoreductase
• Biological source: Streptomyces thioluteus
• Total number of polymer chains: 2
• Total formula weight: 76514.32

Authors

Zhang, H.,Brunzelle, J.S.,Nair, S.K. (deposition date: 2008-03-10, release date: 2008-05-27, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)