嗜热脂肪芽孢杆菌DNA引发酶的克隆、表达与纯化以及锌结合结构域的结晶
Cloning, expression, and purification of Bacillus stearothermophilus DNA primase and crystallization of the zinc-binding domain.
作者信息
Pan H, Bird L E, Wigley D B
机构信息
Sir William Dunn School of Pathology, University of Oxford, South Park Road, Oxford OX1 3RE, UK.
出版信息
Biochim Biophys Acta. 1999 Mar 19;1444(3):429-33. doi: 10.1016/s0167-4781(99)00025-1.
The dnaG gene encoding DNA primase has been isolated from chromosomal DNA of Bacillus stearothermophilus and its entire nucleotide sequence determined. The deduced amino acid sequence comprised 597 amino acid residues and the molecular mass was calculated to be 67068 Da. B. stearothermophilus primase was overexpressed in Escherichia coli and purified to homogeneity. The N-terminal 12 kDa zinc-binding domain has been crystallized. The crystals are of the monoclinic space group P21 with cell dimensions a=36 A, b=59 A, c=46 A, beta=91.8 degrees and diffract to 1.7 A resolution.
编码DNA引发酶的dnaG基因已从嗜热脂肪芽孢杆菌的染色体DNA中分离出来，并测定了其完整的核苷酸序列。推导的氨基酸序列由597个氨基酸残基组成，计算出的分子量为67068道尔顿。嗜热脂肪芽孢杆菌引发酶在大肠杆菌中过量表达并纯化至同质。其N端12 kDa的锌结合结构域已结晶。晶体属于单斜空间群P21，晶胞参数为a = 36 Å，b = 59 Å，c = 46 Å，β = 91.8°，衍射分辨率达1.7 Å。
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