The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria

被引：117

作者：

Aksyuk, Anastasia A. ^{[1
]}

Leiman, Petr G. ^{[1
]}

Kurochkina, Lidia P. ^{[2
]}

Shneider, Mikhail M. ^{[2
]}

Kostyuchenko, Victor A. ^{[1
]}

Mesyanzhinov, Vadim V. ^{[2
]}

Rossmann, Michael G. ^{[1
]}

机构：

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

[2] Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia

来源：

EMBO JOURNAL | 2009年 / 28卷 / 07期

基金：

美国国家科学基金会;

关键词：

bacteriophage T4; cryo-electron microscopy; crystallography; tail sheath contraction; X-RAY-DIFFRACTION; CONTRACTED SHEATH; CRYSTAL-STRUCTURE; PROTEIN; MORPHOGENESIS; MECHANISM;

D O I：

10.1038/emboj.2009.36

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：

The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central noncontractile tail tube. The contraction of the sheath drives the tail tube through the outer membrane, creating a channel for the viral genome delivery. A crystal structure of about three quarters of gp18 has been determined and was fitted into cryo-electron microscopy reconstructions of the tail sheath before and after contraction. It was shown that during contraction, gp18 subunits slide over each other with no apparent change in their structure.

引用

页码：821 / 829

页数：9