A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry
A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry
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DOI：
10.1107/s0907444908004277
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发表时间：
2008-05-01
期刊：
影响因子：
--
通讯作者：
Tsukihara, Tomitake
中科院分区：
文献类型：
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作者：
Kato, Koji;Tanaka, Hideaki;Tsukihara, Tomitake
穹窿是一种分子量为12.9 MDa的核糖核蛋白颗粒，具有桶状形状，两个突出的帽和一个内陷的腰部结构，在多种真核生物中高度保守。主要穹窿蛋白（MVP）的多聚化足以组装桶形穹窿颗粒的整个外壳。另外两种蛋白质的多个拷贝，穹窿多聚（ADP-核糖）聚合酶（VPARP）和端粒酶相关蛋白1（TEP 1），以及小穹窿RNA（vRNA），也与穹窿相关。在这里，拱顶颗粒的结晶报告。晶体属于空间群C2，晶胞参数a = 708.0，B = 385.0，c = 602.9埃，β = 124.8度。基于R因子和非晶体对称性（NCS）平均相关系数的旋转对称性搜索表明，该粒子具有39倍二面角对称性。
Vault is a 12.9 MDa ribonucleoprotein particle with a barrel-like shape, two protruding caps and an invaginated waist structure that is highly conserved in a wide variety of eukaryotes. Multimerization of the major vault protein (MVP) is sufficient to assemble the entire exterior shell of the barrel-shaped vault particle. Multiple copies of two additional proteins, vault poly(ADP-ribose) polymerase (VPARP) and telomerase-associated protein 1 (TEP1), as well as a small vault RNA (vRNA), are also associated with vault. Here, the crystallization of vault particles is reported. The crystals belong to space group C2, with unit-cell parameters a = 708.0, b = 385.0, c = 602.9 angstrom, beta = 124.8 degrees. Rotational symmetry searches based on the R factor and correlation coefficient from noncrystallographic symmetry (NCS) averaging indicated that the particle has 39-fold dihedral symmetry.