Price S, Cusack S, Borel F, Berthet-Colominas C, Leberman R
European Molecular Biology Laboratory, Grenoble Outstation, France.
FEBS Lett. 1993 Jun 14;324(2):167-70. doi: 10.1016/0014-5793(93)81386-e.
Crystals of the complex between seryl-tRNA synthetase and tRNA(2ser) from Escherichia coli have been obtained from ammonium sulphate solutions. The crystals are of the 1:2 enzyme:tRNA complex, belong to the space group C222(1), have cell dimensions of a = 128.9 A, b = 164.9 A, c = 127.3 A and diffract anisotropically from 3.5 to 4.5 A. An X-ray diffraction data set to 4 A has been collected. The combination of molecular replacement using the refined structure of the catalytic domain of the native enzyme, data from a heavy atom derivative and solvent flattening was used to produce a map at 4 A resolution. This shows that a tRNA molecule binds across the dimer, the anticodon stem and loop do not contact the protein and the helical arm of the enzyme contacts the T psi C loop and the long extra arm of the tRNA.
已从硫酸铵溶液中获得了来自大肠杆菌的丝氨酰 - tRNA合成酶与tRNA(2ser)的复合物晶体。这些晶体是1:2的酶:tRNA复合物，属于空间群C222(1)，晶胞参数为a = 128.9 Å，b = 164.9 Å，c = 127.3 Å，并且在3.5至4.5 Å范围内呈现各向异性衍射。已收集到分辨率为4 Å的X射线衍射数据集。使用天然酶催化结构域的精制结构进行分子置换、来自重原子衍生物的数据以及溶剂扁平化相结合的方法，生成了分辨率为4 Å的图谱。这表明一个tRNA分子跨二聚体结合，反密码子茎和环不与蛋白质接触，并且酶的螺旋臂与tRNA的TψC环和长的额外臂接触。
