2GIB

Crystal structure of the SARS coronavirus nucleocapsid protein dimerization domain

2GIB の概要

• エントリーDOI: 10.2210/pdb2gib/pdb
• 分子名称: Nucleocapsid protein, SULFATE ION (3 entities in total)
• 機能のキーワード: sars, nucleocapsid, dimer, viral protein
• 由来する生物種: SARS coronavirus
• 細胞内の位置: Virion: P59595
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23205.82

構造登録者

Yu, I.M.,Oldham, M.L.,Zhang, J.,Chen, J. (登録日: 2006-03-28, 公開日: 2006-04-25, 最終更新日: 2024-02-14)

主引用文献

Yu, I.M.,Oldham, M.L.,Zhang, J.,Chen, J.
Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae.
J.Biol.Chem., 281:17134-17139, 2006

PubMed Abstract: 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 1.75A 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.

PubMed: 16627473
DOI: 10.1074/jbc.M602107200

実験手法

X-RAY DIFFRACTION (1.75 Å)