Three-dimensional structure of the bacteriophage P22 tail machine

EMBO J. 2005 Jun 15;24(12):2087-95. doi: 10.1038/sj.emboj.7600695. Epub 2005 Jun 2.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage P22 / chemistry*
  • Bacteriophage P22 / genetics
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Fourier Analysis
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Viral Tail Proteins / chemistry*
  • Viral Tail Proteins / genetics


  • Viral Tail Proteins