The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein

Lisa G. Pell, Genevieve M.C. Gasmi-Seabrook, Marc Morais, Philipp Neudecker, Voula Kanelis, Diane Bona, Logan W. Donaldson, Aled M. Edwards, P. Lynne Howell, Alan R. Davidson, Karen L. Maxwell

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpVC), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpVC and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpVC by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpVC structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpVC that may be important in mediating the function of this domain.

Original languageEnglish (US)
Pages (from-to)468-479
Number of pages12
JournalJournal of Molecular Biology
Issue number3
StatePublished - Oct 29 2010


  • Bacteriophage lambda
  • GpV
  • Ig-like domain
  • NMR structure
  • Phage tail

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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