Quasi-atomic model of bacteriophage t7 procapsid shell: insights into the structure and evolution of a basic fold

Structure. 2007 Apr;15(4):461-72. doi: 10.1016/j.str.2007.03.004.


The existence of similar folds among major structural subunits of viral capsids has shown unexpected evolutionary relationships suggesting common origins irrespective of the capsids' host life domain. Tailed bacteriophages are emerging as one such family, and we have studied the possible existence of the HK97-like fold in bacteriophage T7. The procapsid structure at approximately 10 A resolution was used to obtain a quasi-atomic model by fitting a homology model of the T7 capsid protein gp10 that was based on the atomic structure of the HK97 capsid protein. A number of fold similarities, such as the fitting of domains A and P into the L-shaped procapsid subunit, are evident between both viral systems. A different feature is related to the presence of the amino-terminal domain of gp10 found at the inner surface of the capsid that might play an important role in the interaction of capsid and scaffolding proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage T7 / chemistry*
  • Bacteriophage T7 / genetics
  • Biological Evolution*
  • Capsid / chemistry*
  • DNA
  • Molecular Sequence Data
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary


  • DNA