酵母糖基磷脂酰肌醇转酰胺酶亚基PIG-S（PIG-S(71-467)）的纯化与结晶
Purification and crystallization of yeast glycosylphosphatidylinositol transamidase subunit PIG-S (PIG-S(71-467)).
作者信息
Kamariah Neelagandan, Eisenhaber Frank, Adhikari Sharmila, Eisenhaber Birgit, Grüber Gerhard
机构信息
Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):896-9. doi: 10.1107/S1744309111024080. Epub 2011 Jul 19.
Abstract
The transfer of glycosylphosphatidylinositol (GPI) anchors onto eukaryotic proteins is catalyzed by the transamidase complex, which is composed of at least five subunits (PIG-K, PIG-S, PIG-T, PIG-U and GPAA1). Here, the recombinant protein PIG-S(71-467) from Saccharomyces cerevisiae, including residues 71-467 of the entire 534-residue protein, was cloned, expressed and purified to homogeneity. The monodisperse protein was crystallized by the vapour-diffusion method. A diffraction data set was collected to 3.2 Å resolution with 91.6% completeness. The crystals belonged to space group C2, with unit-cell parameters a = 106.72, b = 59.33, c = 124.3 Å, β = 114.19°, and contained two molecules in the asymmetric unit.
摘要
糖基磷脂酰肌醇（GPI）锚定到真核蛋白质上的过程由转酰胺酶复合物催化，该复合物至少由五个亚基（PIG-K、PIG-S、PIG-T、PIG-U和GPAA1）组成。在此，来自酿酒酵母的重组蛋白PIG-S(71-467)（包含整个534个残基的蛋白中的71-467位残基）被克隆、表达并纯化至均一性。通过气相扩散法使该单分散蛋白结晶。收集到分辨率为3.2 Å的衍射数据集，完整性为91.6%。晶体属于空间群C2，晶胞参数为a = 106.72、b = 59.33、c = 124.3 Å，β = 114.19°，不对称单位中包含两个分子。
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