Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.

表达式,小鼠肝炎病毒 （ MHV ） 核衣壳蛋白 C 末端结构域的结晶和初步晶体学研究。

• 发表时间: Jun 2010 1
• 来源期刊: Acta Crystallogr Sect F Struct Biol Cryst Commun
• DOI: 10.1107/S1744309110012492
• PMID: 20516597
• 文章类型: Journal Article
• 作者列表: Tong X,Ma Y,Li X

Mesh: Crystallization; Crystallography, X-Ray; Gene Expression; Murine hepatitis virus / chemistry; Nucleocapsid Proteins / chemistry genetics

Abstract

Mouse hepatitis virus (MHV) belongs to the group II coronaviruses. The virus produces nine genes encoding 11 proteins that could be recognized as structural proteins and nonstructural proteins and are crucial for viral RNA synthesis. The nucleocapsid (N) protein, one of the structural proteins, interacts with the 30.4 kb virus genomic RNA to form the helical nucleocapsid and associates with the membrane glycoprotein via its C-terminus to stabilize virion assembly. Here, the expression and crystallization of the MHV nucleocapsid protein C-terminal domain are reported. The crystals diffracted to 2.20 A resolution and belonged to space group P422, with unit-cell parameters a = 66.6, c = 50.8 A. Assuming the presence of two molecules in the asymmetric unit, the solvent content is 43.0% (V(M) = 2.16 A(3) Da(-1)).

摘要

小鼠肝炎病毒(MHV)属于II组冠状病毒。该病毒产生9个基因，编码11种蛋白质，这些蛋白质可被识别为结构蛋白和非结构蛋白，对病毒RNA合成至关重要。核衣壳(N)蛋白,结构蛋白之一，与30.4kb病毒基因组RNA相互作用以形成螺旋核衣壳，并通过其C端与膜糖蛋白缔合以稳定病毒粒子组装。这里,报道了MHV核衣壳蛋白C末端结构域的表达和结晶。晶体衍射至2.20A分辨率，属于空间群P422，晶胞参数a=66.6，c=50.8A。假设不对称单元中存在两个分子，溶剂含量为43.0%(V(M)=2.16A(3)Da(-1))。