Features of reovirus outer capsid protein μ1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Å resolution

被引：60

作者：

Zhang, X

Ji, YC

Zhang, L

Harrison, SC

Marinescu, DC

Nibert, ML ^{[1
]}

Baker, TS

机构：

[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

[2] Univ Cent Florida, Dept Comp Sci, Orlando, FL 32816 USA

[3] Childrens Hosp, Mol Med Lab, Boston, MA 02115 USA

[4] Childrens Hosp, Howard Hughes Med Inst, Boston, MA 02115 USA

[5] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[6] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA

[7] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

[8] Univ Calif San Diego, Dept Biol Mol, La Jolla, CA 92093 USA

来源：

STRUCTURE | 2005年 / 13卷 / 10期

关键词：

D O I：

10.1016/j.str.2005.07.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Reovirus is a useful model for addressing the molecular basis of membrane penetration by one of the larger nonenveloped animal viruses. We now report the structure of the reovirus virion at 7.0 angstrom resolution as obtained by electron cryomicroscopy and three-dimensional image reconstruction. Several features of the myristoylated outer capsid protein mu 1, not seen in a previous X-ray crystal structure of the mu 1-sigma 3 heterohexamer, are evident in the virion. These features appear to be important for stabilizing the outer capsid, regulating the conformational changes in mu 1 that accompany perforation of target membranes, and contributing directly to membrane penetration during cell entry.

引用

页码：1545 / 1557

页数：13

共 55 条

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