Tonozuka Takashi, Uechi Akiko, Mizuno Masahiro, Ichikawa Kazuhiro, Nishikawa Atsushi, Sakano Yoshiyuki
Department of Applied Biological Science, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo 183-8509, Japan.
Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1284-5. doi: 10.1107/S0907444904009631. Epub 2004 Jun 22.
Processing alpha-glucosidase I, which is classified into glycosyl hydrolase (GH) family 63, hydrolyzes an oligosaccharide precursor of eukaryotic N-linked glycoproteins. Recently, many bacteria have been reported to possess genes for proteins that are homologous to the GH family 63 glucosidases. In this paper, Escherichia coli K12 YgjK protein, a member of GH family 63, was overexpressed, purified and crystallized using the vapour-diffusion method. Diffraction data were collected to 1.8 A resolution and the crystal was found to belong to the monoclinic space group P2(1), with unit-cell parameters a = 88.5, b = 137.1, c = 60.9 A, beta = 98.1 degrees. The V(M) value was determined to be 2.1 A(3) Da(-1), which corresponds to the presence of two protein molecules in the asymmetric unit.
加工α-葡萄糖苷酶I（其被归类于糖基水解酶（GH）家族63）可水解真核生物N-连接糖蛋白的寡糖前体。最近，据报道许多细菌拥有与GH家族63葡萄糖苷酶同源的蛋白质基因。在本文中，使用气相扩散法对GH家族63成员大肠杆菌K12 YgjK蛋白进行了过量表达、纯化和结晶。收集了分辨率为1.8 Å的衍射数据，发现该晶体属于单斜空间群P2(1)，晶胞参数为a = 88.5、b = 137.1、c = 60.9 Å，β = 98.1°。V(M)值确定为2.1 ų Da⁻¹，这对应于不对称单元中存在两个蛋白质分子。
