Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
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DOI：
10.1074/jbc.m602107200
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发表时间：
2006-06-23
期刊：
影响因子：
--
通讯作者：
Chen J
中科院分区：
文献类型：
--
作者：
Yu IM;Oldham ML;Zhang J;Chen J
严重急性呼吸系统综合症（SARS）的病原体是SARS相关的冠状病毒SARS- cov。核衣壳蛋白在SARS-CoV基因组包装和病毒粒子组装中起着至关重要的作用。我们之前已经证明，SARS-CoV N蛋白通过其c端结构域在溶液中形成二聚体。在本研究中，由残基270-370组成的二聚化结构域的晶体结构被确定为1.75Å分辨率。该结构显示二聚体在两个亚基之间具有广泛的相互作用，表明二聚体形式的N蛋白是体内的功能单位。SARS-CoV N蛋白的二聚化结构域与猪繁殖与呼吸综合征病毒的核衣壳蛋白具有相似的折叠，但缺乏明显的序列相似性。这一发现为冠状病毒科和动脉病毒科之间的进化联系提供了结构证据，表明两种病毒的N蛋白具有共同的起源。
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly. We have previously shown that SARS-CoV N protein forms a dimer in solution through its C-terminal domain. In this study, the crystal structure of the dimerization domain, consisting of residues 270–370, is determined to 1.75Å resolution. The structure shows a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo. Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus. This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin.