1H - 3 - 羟基 - 4 - 氧代喹啉2,4 - 双加氧酶的结晶与衍射数据：α/β - 水解酶家族的一种无辅因子加氧酶
Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family.
作者信息
Qi Ruhu, Fetzner Susanne, Oakley Aaron J
机构信息
Research School of Chemistry, Australian National University, Acton, ACT 0200, Australia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):378-81. doi: 10.1107/S1744309107013760. Epub 2007 Apr 6.
Abstract
1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 catalyses the oxygenolysis of 1H-3-hydroxy-4-oxoquinoline to form N-formylanthranilic acid and carbon monoxide without the aid of cofactors. Both N-terminally His6-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His6-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6(1)22. Selenomethionine-containing native QDO was prepared and crystallized under identical conditions. The unit-cell parameters were a = b = 90.1, c = 168.6 A, alpha = beta = 90, gamma = 120 degrees. Using synchrotron radiation, these crystals diffract to 2.5 A. The expression, purification and crystallization of QDO are reported here.
摘要
恶臭假单胞菌33/1中的1H-3-羟基-4-氧代喹啉2,4-双加氧酶（QDO）在无辅因子的情况下催化1H-3-羟基-4-氧代喹啉的氧解反应，生成N-甲酰基邻氨基苯甲酸和一氧化碳。N端带有His6标签的QDO和天然QDO均在大肠杆菌中过表达，并通过常规色谱方法进行纯化。未标记的QDO（而非His6标签标记的QDO）通过气相扩散法结晶，得到属于空间群P6(1)22的六方双锥晶体。制备了含硒代甲硫氨酸的天然QDO，并在相同条件下结晶。晶胞参数为a = b = 90.1，c = 168.6 Å，α = β = 90°，γ = 120°。利用同步辐射，这些晶体的衍射分辨率达到2.5 Å。本文报道了QDO的表达、纯化及结晶情况。
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