Three-dimensional structure of the bacteriophage P22 tail machine

被引:61
|
作者
Tang, L
Marion, WR
Cingolani, G
Prevelige, PE
Johnson, JE
机构
[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[2] Univ Alabama Birmingham, Dept Microbiol, Birmingham, AL 35294 USA
来源
EMBO JOURNAL | 2005年 / 24卷 / 12期
关键词
bacteriophage; electron cryo-microscopy; molecular machine; symmetry; tail;
D O I
10.1038/sj.emboj.7600695
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 tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation.
引用
收藏
页码:2087 / 2095
页数:9
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