Open AccessCrystallization and preliminary crystallographic analysis of 2‐aminophenol 1,6‐dioxygenase complexed with substrate and with an inhibitor
Author(s) -
Li DeFeng,
Zhang JiaYue,
Hou Yanjie,
Liu Lei,
Liu ShuangJiang,
Liu Wei
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112038705
Subject(s) - dioxygenase , crystallization , crystallography , chemistry , substrate (aquarium) , catechol , carboxylate , stereochemistry , enzyme , resolution (logic) , x ray crystallography , crystal (programming language) , crystal structure , diffraction , organic chemistry , biology , ecology , programming language , physics , artificial intelligence , computer science , optics
Dioxygen activation implemented by nonhaem Fe II enzymes containing the 2‐His‐1‐carboxylate facial triad has been extensively studied in recent years. Extradiol dioxygenase is the archetypal member of this superfamily and catalyzes the oxygenolytic ring opening of catechol analogues. Here, the crystallization and preliminary X‐ray analysis of 2‐aminophenol 1,6‐dioxygenase, an enzyme representing a minor subset of extradiol dioxygenases that catalyze the fission of 2‐aminophenol rather than catecholic compounds, is reported. Crystals of the holoenzyme with Fe II and of complexes with the substrate 2‐aminophenol and the suicide inhibitor 4‐nitrocatechol were grown using the cocrystallization method under the same conditions as used for the crystallization of the apoenzyme. The crystals belonged to space group C 2 and diffracted to 2.3–2.7 Å resolution; the crystal that diffracted to the highest resolution had unit‐cell parameters a = 270.24, b = 48.39, c = 108.55 Å, β = 109.57°. All X‐ray data sets collected from diffraction‐quality crystals were suitable for structure determination.