Expression, purification, crystallization and preliminary X-ray analysis of para-nitrophenol 4-monooxygenase from Pseudomonas putida DLL-E4.
Para-nitrophenol 4-monooxygenase (PnpA) plays an important role in bacterial degradation of para-nitrophenol by oxidative release of the nitro group from the aromatic ring to form p-benzoquinone. In order to understand the structural basis of the function of this enzyme, PnpA was cloned, expressed in Escherichia coli and purified. PnpA was crystallized by the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The PnpA crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.47, b = 77.56, c = 209.17 A, and diffracted to 2.24 A resolution.
Liu
Weidong
W
Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural University, 210095 Nanjing, People's Republic of China.
Shen
Wenjing
W
Zhao
Xiaoli
X
Cao
Hui
H
Cui
Zhongli
Z
D003460:Crystallization; D018360:Crystallography, X-Ray; D010105:Oxygenases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D016958:Pseudomonas putida / Q000201:enzymology*
D010105:Oxygenases; C113515:4-nitrophenol monooxygenase