Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages.

Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages.
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DOI:
10.1016/j.jmb.2009.10.007
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发表时间:
2010-01-29
影响因子:
5.6
通讯作者:
Rossmann MG
Rossmann MG
中科院分区:
生物学2区
文献类型:
--
作者:
Qin L;Fokine A;O'Donnell E;Rao VB;Rossmann MG

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许多病毒需要稳定其衣壳结构以抵抗DNA压力并在恶劣环境中生存。稳定病毒的噬菌体T4的9 kDa外衣壳蛋白(Soc)在成熟的最后阶段附着在衣壳上。有870个Soc分子在相邻的六聚体壳粒之间充当“胶水”,形成一个“笼子”,使T4衣壳稳定,免受极端pH和温度的影响。在这里,我们报告了一个1.9纳米分辨率的晶体结构的Soc从噬菌体RB69,T4的近亲。RB69晶体结构和T4 Soc的同源性模型被拟合到T4衣壳的冷冻电镜重建中。这建立了与主要衣壳蛋白相互作用的Soc区域,并提出了一种机制,通过广泛的突变和生物化学研究验证,用于稳定衣壳,其中Soc三聚体作为相邻衣壳之间的夹子。结果表明,不仅T4样噬菌体的衣壳,而且许多其他病毒衣壳的稳定化所涉及的因素。
Many viruses need to stabilize their capsid structure against DNA pressure and for survival in hostile environments. The 9 kDa outer capsid protein (Soc) of bacteriophage T4, which stabilizes the virus, attaches to the capsid during the final stage of maturation. There are 870 Soc molecules that act as “glue” between neighboring hexameric capsomers, forming a “cage” that stabilizes the T4 capsid against extremes of pH and temperature. Here we report a 1.9 Å resolution crystal structure of Soc from the bacteriophage RB69, a close relative of T4. The RB69 crystal structure and a homology model of T4 Soc were fitted into the cryo-electron microscopy reconstruction of the T4 capsid. This established the region of Soc that interacts with the major capsid protein and suggested a mechanism, verified by extensive mutational and biochemical studies, for stabilization of the capsid in which the Soc trimers act as clamps between neighboring capsomers. The results demonstrate the factors involved in stabilizing not only the capsids of T4-like bacteriophages but also many other virus capsids.
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