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首页> 外文期刊>Journal of Molecular Biology >Canine Parvovirus Capsld Structure, Analyzed at 2.9 A Resolution
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Canine Parvovirus Capsld Structure, Analyzed at 2.9 A Resolution

机译：犬细小病毒Capsld结构，以2.9 A分辨率分析

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摘要

The DNA-containing capsid of canine parvovirus (CPV) is analysed following atomic refinement at 2.9 A resolution. The capsid contains 60 copies of the capsid protein related by icosahedral symmetry. The atomic model has been extended from the first residue (Gly37) of the unrefined 3.25 A structure towards the N terminus. The electron density shows that - 87% of the capsid proteins have N termini on the inside of the capsid, but for - 13%, the polypeptide starts on the outside and runs through one ofthe pores surrounding each 5-fold axis, explaining apparently conflicting antigenic data. Analysis of potential hydrogen bonds reveals -50% more secondary structure than previously apparent. Most of the additional secondary structure are in the 71 and 221 residue-long loop insertions between p-strands E and F and G and H, forming subunit-bridging sheets that likely add specificity to assembly interactions. Structural analysis of the extensive subonit interactions around the 3-fold axes shows that assembly is a multistep process with loops intertwining following initial contact. Estimated free energies of association suggest that the formation of 3 and 5-fold contacts Likely takes precedence over 2-fold interactions. Energies for initial association into trimers or pentamers would be similar, but the intertwining of loops about the 3-fold axis adds an additional large activation barrier to dissociation. Analysis of the surfaces of the assembled capsid shows a surprising lack of basic amino acids that might have been expected to interact with the negatively charged phosphoribose backbone of the DNA. Instead, uncharged polar and van der Waal's interactions predominate in the packaging of single-stranded DNA into the capsid.
机译：以2.9 A的分辨率对原子细化后的犬细小病毒（CPV）的DNA衣壳进行了分析。衣壳包含通过二十面体对称性相关的衣壳蛋白的60个拷贝。原子模型已从未精制的3.25 A结构的第一个残基（Gly37）延伸至N末端。电子密度表明-87％的衣壳蛋白在衣壳内部具有N末端，但对于-13％的衣壳蛋白，该多肽从外部开始并穿过每个5倍轴周围的孔之一，这显然表明存在冲突抗原数据。潜在氢键的分析显示，二级结构比以前明显多出-50％。大多数其他二级结构位于p链E和F与G和H之间的71和221个残基长的环插入中，形成亚单位桥接片，这可能会增加装配相互作用的特异性。对围绕3折轴的大量subonit相互作用的结构分析表明，组装是一个多步骤的过程，在初始接触之后，环缠绕在一起。估计的缔合自由能表明3和5倍接触的形成可能优先于2倍相互作用。初始结合成三聚体或五聚体的能量将是相似的，但是围绕3折轴的环交织会增加解离的额外激活障碍。对组装的衣壳表面的分析表明，令人惊讶地缺乏碱性氨基酸，这些碱性氨基酸可能被期望与DNA带负电荷的磷酸核糖主链相互作用。相反，不带电荷的极性和范德华的相互作用在将单链DNA装入衣壳中的过程中占主导地位。

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