Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures

Cell. 1999 Sep 17;98(6):825-33. doi: 10.1016/s0092-8674(00)81516-0.


The unusual bacteriophage PRD1 features a membrane beneath its icosahedral protein coat. The crystal structure of the major coat protein, P3, at 1.85 A resolution reveals a molecule with three interlocking subunits, each with two eight-stranded viral jelly rolls normal to the viral capsid, and putative membrane-interacting regions. Surprisingly, the P3 molecule closely resembles hexon, the equivalent protein in human adenovirus. Both viruses also have similar overall architecture, with identical capsid lattices and attachment proteins at their vertices. Although these two dsDNA viruses infect hosts from very different kingdoms, their striking similarities, from major coat protein through capsid architecture, strongly suggest their evolutionary relationship.

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

  • Adenoviruses, Human / chemistry
  • Amino Acid Sequence
  • Capsid / chemistry*
  • Capsid Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • Evolution, Molecular
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Synchrotrons
  • Tectiviridae / chemistry*


  • Capsid Proteins
  • hexon capsid protein, Adenovirus
  • protein P3, bacteriophage PRD1

Associated data

  • PDB/1CJD