The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p

Nat Struct Biol. 1998 Feb;5(2):140-7. doi: 10.1038/nsb0298-140.


The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Capsid Proteins
  • Crystallography, X-Ray / methods*
  • DNA-Binding Proteins / chemistry*
  • Inovirus / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Library*
  • Protein Conformation*
  • Selenomethionine
  • Sequence Homology, Amino Acid
  • Viral Fusion Proteins / chemistry*


  • Capsid Proteins
  • DNA-Binding Proteins
  • Peptide Library
  • Viral Fusion Proteins
  • Selenomethionine

Associated data

  • PDB/1G3P