Liang Yu-He, Liu Xiang-Yu, Wang Juan, Li Lan-Fen
The National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):709-11. doi: 10.1107/S1744309109020703. Epub 2009 Jun 27.
Glycinamide ribonucleotide transformylase (GART) catalyzes the transfer of a formyl group from formyl tetrahydrofolate (FTHF) to glycinamide ribonucleotide (GAR), which is an essential step in the de novo synthesis pathway of purines. In Bacillus subtilis, GART is encoded by the gene purN. In order to study the structure and function of B. subtilis GART, the purN gene was amplified, cloned into an expression vector and expressed in soluble form in Escherichia coli. The protein was purified to homogeneity and crystals suitable for X-ray data collection were obtained. These crystals diffracted to 2.5 A resolution and belonged to space group P3(1)21, with unit-cell parameters a = b = 95.5, c = 64.0 A.
甘氨酰胺核苷酸转甲酰基酶(GART)催化甲酰基从甲酰四氢叶酸(FTHF)转移至甘氨酰胺核苷酸(GAR),这是嘌呤从头合成途径中的关键步骤。在枯草芽孢杆菌中,GART由purN基因编码。为研究枯草芽孢杆菌GART的结构与功能,扩增了purN基因,将其克隆至表达载体并在大肠杆菌中以可溶形式表达。该蛋白经纯化达到均一性,并获得了适合X射线数据收集的晶体。这些晶体的衍射分辨率为2.5 Å,属于空间群P3(1)21,晶胞参数a = b = 95.5,c = 64.0 Å。