Minor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid

Nat Struct Biol. 2002 Oct;9(10):756-63. doi: 10.1038/nsb837.


Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.

Publication types

  • 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

  • Bacteriophage PRD1 / genetics
  • Bacteriophage PRD1 / metabolism*
  • Capsid / metabolism*
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Intracellular Membranes / metabolism
  • Models, Molecular

Associated data

  • PDB/1GW7
  • PDB/1GW8