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J. Biol. Chem., Vol. 281, Issue 25, 17134-17139, June 23, 2006

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Crystal Structure of the Severe Acute Respiratory Syndrome (SARS) Coronavirus Nucleocapsid Protein Dimerization Domain Reveals Evolutionary Linkage between Corona- and Arteriviridae^*

I-Mei Yu¹, Michael L. Oldham¹, Jingqiang Zhang, and Jue Chen²

From the Department of Biological Sciences and the Cancer Center, Purdue University, West Lafayette, Indiana 47907 and the State Key Laboratory for Biocontrol, Zhongshan University, Guangzhou 510275, China

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.

Received for publication, March 6, 2006 , and in revised form, April 11, 2006.

^* This work was supported by National Institutes of Health Grant P01 AI055672 (to R. J. K.) and by a grant from the Pew Scholars Program in the Biomedical Sciences (to J. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 2GIB) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 765-496-3113; Fax: 765-496-1189; E-mail: chenjue{at}purdue.edu.

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