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首页> 外文期刊>Journal of Molecular Biology >A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80alpha capsids.
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A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80alpha capsids.

机译：构型转换参与金黄色葡萄球菌噬菌体80alpha衣壳的成熟。

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摘要

Bacteriophages are involved in many aspects of the spread and establishment of virulence factors in Staphylococcus aureus, including the mobilization of genetic elements known as S. aureus pathogenicity islands (SaPIs), which carry genes for superantigen toxins and other virulence factors. SaPIs are packaged into phage-like transducing particles using proteins supplied by the helper phage. We have used cryo-electron microscopy and icosahedral reconstruction to determine the structures of the procapsid and the mature capsid of 80alpha, a bacteriophage that can mobilize several different SaPIs. The 80alpha capsid has T=7 icosahedral symmetry with the capsid protein organized into pentameric and hexameric clusters that interact via prominent trimeric densities. The 80alpha capsid protein was modeled based on the capsid protein fold of bacteriophage HK97 and fitted into the 80alpha reconstructions. The models show that the trivalent interactions are mediated primarily by a 22-residue beta hairpin structure called the P loop that is not found in HK97. Capsid expansion is associated with a conformational switch in the spine helix that is propagated throughout the subunit, unlike the domain rotation mechanism in phage HK97 or P22.
机译：噬菌体涉及金黄色葡萄球菌中毒力因子的传播和建立的许多方面，包括动员称为金黄色葡萄球菌致病性岛（SaPIs）的遗传元件的携带，这些遗传元件携带超抗原毒素和其他毒力因子的基因。使用辅助噬菌体提供的蛋白质将SaPIs包装到噬菌体样转导颗粒中。我们已经使用了冷冻电子显微镜和二十面体重建来确定前壳和80alpha的成熟衣壳的结构，80alpha是一种可以动员几种不同SaPI的噬菌体。 80alpha衣壳具有T = 7二十面体对称性，衣壳蛋白组织成五聚体和六聚体簇，它们通过显着的三聚体密度相互作用。基于噬菌体HK97的衣壳蛋白折叠来模拟80alpha衣壳蛋白，并将其装配到80alpha重组体中。该模型显示，三价相互作用主要是由22个残基的β发夹结构（称为P环）介导的，该结构在HK97中找不到。与噬菌体HK97或P22中的域旋转机制不同，衣壳扩展与在整个亚基中传播的脊柱螺旋中的构象转换有关。

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