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TitleThree-dimensional structure of the bacteriophage P22 tail machine.
Journal, issue, pagesEMBO J, Vol. 24, Issue 12, Page 2087-2095, Year 2005
Publish dateJun 15, 2005
AuthorsLiang Tang / William R Marion / Gino Cingolani / Peter E Prevelige / John E Johnson /
PubMed AbstractThe 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- ...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.
External linksEMBO J / PubMed:15933718 / PubMed Central
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-1119:
Three-dimensional structure of the bacteriophage P22 tail machine.
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Enterobacteria phage P22 (virus)

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