Structural conservation of the myoviridae phage tail sheath protein fold

Structure. 2011 Dec 7;19(12):1885-94. doi: 10.1016/j.str.2011.09.012.


Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 Å resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 Å resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4.

Publication types

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

MeSH terms

  • Bacteriophage T4 / chemistry
  • Bacteriophage T4 / metabolism
  • Crystallography, X-Ray
  • Microscopy, Electron
  • Myoviridae / chemistry*
  • Myoviridae / metabolism
  • Protein Conformation
  • Protein Folding
  • Viral Tail Proteins / chemistry*


  • Viral Tail Proteins

Associated data

  • PDB/3HXL
  • PDB/3JOH
  • PDB/3JOI
  • PDB/3LML
  • PDB/3SPE