Ludwig Kai, Baljinnyam Bolormaa, Herrmann Andreas, Böttcher Christoph
Forschungszentrum für Elektronenmikroskopie, Freie Universität Berlin, Berlin, Germany.
EMBO J. 2003 Aug 1;22(15):3761-71. doi: 10.1093/emboj/cdg385.
The three dimensional (3D) structure of the ectodomain of the entire fusion mediating F protein from Sendai virus [MW (trimer) approximately 177 kDa] has been determined by cryoelectron microscopy of single molecules and subsequent 3D reconstruction at a resolution of approximately 16 A. The reconstruction, which has been obtained from the native, proteolytic processed fusion primed F1+F2 form, shows the protein protruding approximately 170 A out of the membrane in a homotrimeric association. It consists of a defined approximately 65 A wide distal head and an adjacent neck, which is connected to an 70 A elongated stalk. Although the overall shape appears to be similar to the recently reported X-ray structure of the Newcastle disease virus F protein, a closer comparison reveals structural differences suggesting that the investigated Sendai F structure represents an advanced state towards the fusion active conformation.
通过单分子冷冻电子显微镜及随后约16埃分辨率的三维重建,已确定了来自仙台病毒的介导融合的F蛋白胞外域的三维(3D)结构[分子量(三聚体)约177 kDa]。该重建是从天然的、经蛋白酶处理的融合引发的F1+F2形式获得的,显示该蛋白以同三聚体形式从膜中突出约170埃。它由一个确定的约65埃宽的远端头部和一个相邻的颈部组成,颈部连接到一个70埃长的柄部。尽管总体形状似乎与最近报道的新城疫病毒F蛋白的X射线结构相似,但更仔细的比较揭示了结构差异,这表明所研究的仙台F结构代表了向融合活性构象发展的一个高级状态。