Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications

Nature. 1992 Jan 9;355(6356):137-43. doi: 10.1038/355137a0.


The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage phi X174. The F protein forms a T = 1 capsid whose major folding motif is the eight-stranded antiparallel beta barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight beta barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure,

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage phi X 174 / chemistry
  • Bacteriophage phi X 174 / genetics
  • Bacteriophage phi X 174 / ultrastructure*
  • Capsid / chemistry
  • DNA, Viral / chemistry
  • DNA, Viral / metabolism
  • Ion Channels / chemistry
  • Ion Channels / metabolism
  • Molecular Sequence Data
  • Molecular Structure
  • Mutation
  • Protein Conformation
  • Viral Proteins / chemistry
  • Viral Structural Proteins / chemistry*
  • Viral Structural Proteins / genetics
  • Viral Structural Proteins / metabolism
  • X-Ray Diffraction


  • DNA, Viral
  • Ion Channels
  • Viral Proteins
  • Viral Structural Proteins