Molecular architecture of the prolate head of bacteriophage T4
Molecular architecture of the prolate head of bacteriophage T4
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DOI：
10.1073/pnas.0400444101
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发表时间：
2004-04-20
影响因子：
11.1
通讯作者：
Rossmann, MG
中科院分区：
文献类型：
--
作者：
Fokine, A;Chipman, PR;Rossmann, MG
T4噬菌体的头部是一个长二十面体，有一个独特的入口顶点，噬菌体尾部附着在这个顶点上。利用低温电子显微镜测定了成熟T4噬菌体头部的三维结构，分辨率为22埃。T4衣壳具有六边形的表面晶格，其特征为三角形数T-end = 13 laevo为二十面体帽，T-mid = 20为中段。主要的衣壳蛋白基因产物（gp）23*的六聚体和顶点蛋白gp24*的五聚体，以及高抗原性的外衣壳蛋白（hoc）和小外衣壳蛋白（soc）的外表面蛋白在重建中清晰可见。gp23*六聚体的大小和形状与噬菌体HK97的主要衣壳蛋白组织相似。通过对soc（-）和hoc(-)soc(-) T4结构的分析，确定了hoc蛋白和soc蛋白的结合位点和形状。
The head of bacteriophage T4 is a prolate icosahedron with one unique portal vertex to which the phage tail is attached. The three-dimensional structure of mature bacteriophage T4 head has been determined to 22-Angstrom resolution by using cryo-electron microscopy. The T4 capsid has a hexagonal surface lattice characterized by the triangulation numbers T-end = 13 laevo for the icosahedral caps and T-mid = 20 for the midsection. Hexamers of the major capsid protein gene product (gp)23* and pentamers of the vertex protein gp24*, as well as the outer surface proteins highly antigenic outer capsid protein (hoc) and small outer capsid protein (soc), are clearly evident in the reconstruction. The size and shape of the gp23* hexamers are similar to the major capsid protein organization of bacteriophage HK97. The binding sites and shape of the hoc and soc proteins have been established by analysis of the soc(-) and hoc(-)soc(-) T4 structures.