Tang Liang, Marion William R, Cingolani Gino, Prevelige Peter E, Johnson John E
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
EMBO J. 2005 Jun 15;24(12):2087-95. doi: 10.1038/sj.emboj.7600695. Epub 2005 Jun 2.
The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation.
噬菌体P22的尾部由多种蛋白质成分组成，并整合了对噬菌体组装和感染至关重要的各种生物学功能。通过电子冷冻显微镜和图像重建确定的P22尾部机器的三维结构揭示了以51个亚基形式存在的五种多肽如何通过十二重、六重和三重对称性组装成这个分子机器，并为宿主细胞附着和噬菌体DNA转运过程中的分子事件提供了见解。
