Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus.
Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus.
复制标题
双链 DNA 病毒支架蛋白外壳蛋白结合域的结构。
DOI：
10.1006/jmbi.2000.3620
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Krishna,NR
中科院分区：
文献类型：
--
作者：
Sun,Y;Parker,MH;Weigele,P;Casjens,S;PreveligeJr,PE;Krishna,NR
支架蛋白是大多数高T数dsDNA病毒如大型噬菌体和疱疹病毒家族的高保真组装所必需的。它们通过在衣壳组装过程中瞬时结合和定位外壳蛋白亚基来发挥功能。在噬菌体P22和疱疹病毒中，极端支架C末端高度带电，预测为两亲性α-螺旋，并且足以结合外壳蛋白，表明共同的作用模式。核磁共振研究表明，P22支架蛋白的外壳蛋白结合结构域表现出螺旋-环-螺旋基序稳定的疏水核心。基序的一面的特征在于高密度的正电荷，其可以通过静电相互作用与外壳蛋白相互作用。从以前的研究与截断片段和所观察到的组装过程中的盐敏感性的NMR结构解释的结果。
Scaffolding proteins are required for high fidelity assembly of most high T number dsDNA viruses such as the large bacteriophages, and the herpesvirus family. They function by transiently binding and positioning the coat protein subunits during capsid assembly. In both bacteriophage P22 and the herpesviruses the extreme scaffold C terminus is highly charged, is predicted to be an amphipathic α-helix, and is sufficient to bind the coat protein, suggesting a common mode of action. NMR studies show that the coat protein-binding domain of P22 scaffolding protein exhibits a helix-loop-helix motif stabilized by a hydrophobic core. One face of the motif is characterized by a high density of positive charges that could interact with the coat protein through electrostatic interactions. Results from previous studies with a truncation fragment and the observed salt sensitivity of the assembly process are explained by the NMR structure.