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首页> 外文期刊>Journal of Molecular Biology >Structure of Mutant Hepatitis B Core Protein Capsids with Premature Secretion Phenotype
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Structure of Mutant Hepatitis B Core Protein Capsids with Premature Secretion Phenotype

机译：突变体乙型肝炎核心蛋白衣壳的结构早熟分泌表型

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Hepatitis B virus is a major human pathogen that consists of a viral genome surrounded by an icosahedrally ordered core protein and a polymorphic, lipidic envelope that is densely packed with surface proteins. A point mutation in the core protein in which a phenylalanine at position 97 is exchanged for a smaller leucine leads to premature envelopment of the capsid before the genome maturation is fully completed. We have used electron cryo-microscopy,rid image processing to investigate how the point mutation affects the structure of the capsid at 2.6- to 2.8 angstrom-resolution. We found that in the mutant the smaller side chain at position 97 is displaced, increasing the size of an adjacent pocket in the center of the spikes of the capsid. In the mutant, this pocket is filled with an unknown density. Phosphorylation of serine residues in the unresolved C-terminal domain of the mutant leaves the structure of the ordered capsid largely unchanged. However, we were able to resolve several previously unresolved residues downstream of proline 144 that precede the phosphorylationsites. These residues pack against the neighboring subunits and increase the inter-dimer contact suggesting that the C-termini play an important role in capsid stabilization and provide a much larger interaction interface than previously observed. (C) 2018 Elsevier Ltd. All rights reserved.
机译：乙型肝炎病毒是主要的人类病原体，它由一个病毒基因组由icosahedrally有序核心蛋白和被致密地填充有表面蛋白的多态，脂质包膜包围的。其中第97位苯丙氨酸被用于更小的亮氨酸导致基因组的成熟前衣壳的过早包络交换的核心蛋白的点突变被完全完成。我们用低温电子显微，摆脱图像处理，调查点突变如何影响衣壳在2.6-结构，以2.8埃的分辨率。我们发现，在突变体的更小的侧链97的位置发生位移，在衣壳的尖峰的中心增加一个相邻口袋的大小。在突变体中，这个口袋充满了未知的密度。在突变体叶的有序衣壳的结构基本不变的未解决的C端结构域的丝氨酸残基的磷酸化。然而，我们能够解决先于phosphorylationsites脯氨酸144的下游几个以前没有解决的残留物。这些残基包靠在相邻亚基和增加帧间二聚体接触这表明C-末端起到衣壳稳定性的重要作用，并提供了比以前观察到的大得多的交互界面。 （c）2018年elestvier有限公司保留所有权利。

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