Insights into assembly from structural analysis of bacteriophage PRD1
Insights into assembly from structural analysis of bacteriophage PRD1
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DOI：
10.1038/nature03056
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发表时间：
2004-11-04
期刊：
影响因子：
64.8
通讯作者：
Bamford, JKH
中科院分区：
文献类型：
--
作者：
Abrescia, NGA;Cockburn, JJB;Bamford, JKH
含膜噬菌体PRD 1的结构已通过X射线晶体学在约4埃分辨率下确定。在这里，我们描述了蛋白质P3，P16，P30和P31的结构和位置。不同的结构蛋白似乎在控制病毒装配中具有专门的作用。线性延伸的P30似乎使二十面体刻面（由主要衣壳蛋白P3的三聚体组成）的形成成核，并充当分子带测量，定义病毒的大小并将刻面粘合在一起。P31的五聚体形成顶点碱基，与P3的亚基互锁并与膜蛋白P16相互作用。与腺病毒和已知最大的病毒颗粒之一PBCV-1的结构相似性支持了PRD 1的组装机制是可缩放的并且适用于由这些病毒形成的主要病毒谱系的观点。
The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 Angstrom resolution. Here we describe the structure and location of proteins P3, P16, P30 and P31. Different structural proteins seem to have specialist roles in controlling virus assembly. The linearly extended P30 appears to nucleate the formation of the icosahedral facets ( composed of trimers of the major capsid protein, P3) and acts as a molecular tape-measure, defining the size of the virus and cementing the facets together. Pentamers of P31 form the vertex base, interlocking with subunits of P3 and interacting with the membrane protein P16. The architectural similarities with adenovirus and one of the largest known virus particles PBCV-1 support the notion that the mechanism of assembly of PRD1 is scaleable and applies across the major viral lineage formed by these viruses.