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Three‐dimensional structure of the bacteriophage P22 tail machine
Author(s) -
Tang Liang,
Marion William R,
Cingolani Gino,
Prevelige Peter E,
Johnson John E
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600695
Subject(s) - biology , bacteriophage , computational biology , genetics , evolutionary biology , escherichia coli , gene
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.