Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that damage recognizes oxidative DNA damage
Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that damage recognizes oxidative DNA damage
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DOI：
10.1107/s0907444904007929
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发表时间：
2004-06-01
影响因子：
2.2
通讯作者：
Doublié, S
中科院分区：
文献类型：
--
作者：
Bandaru, V;Cooper, W;Doublié, S
DNA糖基化酶修复由自由基引起的氧化DNA损伤。最近，NEIL 1，大肠杆菌DNA糖基化酶内切核酸酶VIII的人类同源物，已被确定，并显示出广泛的底物特异性的各种类型的嘧啶碱基损伤。在大肠杆菌中过量表达NEIL 1的C末端缺失的活性结构。大肠杆菌并结晶。未配体的NEIL 1晶体属于空间群R3，晶胞参数a=B=132.2，c=51.1埃。从天然的、硒代甲硫酰和碘化的NEIL 1分别收集到2.1、2.3和2.4埃的完整数据集。
DNA glycosylases repair oxidative DNA damage caused by free radicals. Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types of pyrimidine-base damage. An active C-terminal deletion construct of NEIL1 was overexpressed in E. coli and crystallized. The unliganded NEIL1 crystallizes in space group R3, with unit-cell parameters a=b=132.2, c=51.1 Angstrom. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4 Angstrom, respectively.