Crystal structure of the matrix protein VP40 from Ebola virus
Crystal structure of the matrix protein VP40 from Ebola virus
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埃博拉病毒基质蛋白 VP40 的晶体结构
DOI：
10.1093/emboj/19.16.4228
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发表时间：
2000-08-15
期刊：
影响因子：
11.4
通讯作者：
Weissenhorn, W
中科院分区：
文献类型：
--
作者：
Dessen, A;Volchkov, V;Weissenhorn, W
埃博拉病毒成熟发生在感染细胞的质膜上，涉及病毒基质蛋白VP 40在组装位点的聚集以及其与脂质双层的相互作用。在这里，我们报告了埃博拉病毒VP 40的X射线晶体结构，分辨率为2.0埃。晶体结构显示，埃博拉病毒VP 40在拓扑结构上不同于所有其他已知的病毒基质蛋白，由具有独特折叠的两个结构域组成，通过柔性接头连接。膜结合所必需的C-末端结构域包含大的疏水性斑块，其可能参与与脂质双层的相互作用。同样，两个结构域之间共享高度碱性区域。晶体结构揭示了分子如何能够从单体构象转换为六聚体形式，如在体外观察到的。它的装配过程中的影响进行了讨论。
Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 Angstrom resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers, Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.