Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion
Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion
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DOI：
10.1093/emboj/20.7.1485
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发表时间：
2001-04-02
期刊：
影响因子：
11.4
通讯作者：
Rey, FA
中科院分区：
文献类型：
--
作者：
Mathieu, M;Petitpas, I;Rey, FA
轮状病毒是引起儿童严重胃肠炎的重要病原体，其结构蛋白VP 6是病毒三层衣壳的中间层。本文报道了VP 6的晶体结构，并通过将原子模型拟合到病毒粒子的冷冻显微镜重建中来描述其与其他衣壳蛋白的相互作用。形成紧密三聚体的VP 6具有两个不同的结构域：远端β-桶结构域和近端α-螺旋结构域，它们分别与病毒粒子的外层和内层相互作用.总体折叠类似于来自蓝舌病病毒的蛋白VP 7的折叠，其中亚基围绕中心3倍轴包裹。VP 6三聚体的一个显著特征是位于3重分子轴上的中心Zn 2+离子。从拟合得到的中间层的粗原子模型表明，在T = 13中间层中VP 6仅部分遵守准等效性，并提出了将260个VP 6三聚体组装到T = 1病毒内层上的模型。
The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid, Here we present the crystal structure of VP6 determined to 2 Angstrom resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta -barrel domain and a proximal alpha -helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis. A distinguishing feature of the VP6 trimer is a central Zn2+ ion located on the 3-fold molecular axis. The crude atomic model of the middle layer derived from the fit shows that quasi-equivalence is only partially obeyed by VP6 in the T = 13 middle layer and suggests a model for the assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.