Walleczek J, Schüler D, Stöffler-Meilicke M, Brimacombe R, Stöffler G
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, FRG.
EMBO J. 1988 Nov;7(11):3571-6. doi: 10.1002/j.1460-2075.1988.tb03234.x.
A three-dimensional model for the arrangement of 29 of the 33 proteins from the Escherichia coli large ribosomal subunit has been generated by interactive computer graphics. The topographical information that served as input in the model building process was obtained by combining the immunoelectron microscopically determined network of epitope-epitope distances on the surface of the large ribosomal subunit with in situ protein-protein cross-linking data. These two independent sets of data were shown to be compatible by geometric analysis, thus allowing the construction of an inherently consistent model. The model shows (i) that the lower third of the large subunit is protein-poor, (ii) that proteins known to be functionally involved in peptide bond formation and translocation are clustered in two separate regions, (iii) that proteins functionally interdependent during the self-assembly of the large subunit are close neighbours in the mature subunit and (iv) that proteins forming the early assembly nucleus are grouped together in a distinct region at the 'back' of the subunit.
通过交互式计算机图形技术生成了大肠杆菌大核糖体亚基33种蛋白质中29种蛋白质排列的三维模型。在模型构建过程中作为输入的拓扑信息是通过将免疫电子显微镜确定的大核糖体亚基表面表位 - 表位距离网络与原位蛋白质 - 蛋白质交联数据相结合而获得的。通过几何分析表明这两组独立的数据是兼容的，从而允许构建一个内在一致的模型。该模型显示：（i）大亚基的下三分之一蛋白质含量低；（ii）已知在肽键形成和转位中起功能作用的蛋白质聚集在两个独立的区域；（iii）在大亚基自组装过程中功能相互依赖的蛋白质在成熟亚基中是紧密相邻的邻居；（iv）形成早期组装核的蛋白质在亚基“背面”的一个独特区域中聚集在一起。
