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 β-strands and a single α-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 ?. 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.
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Lubkowski, J., Hennecke, F., Plückthun, A. et al. The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p. Nat Struct Mol Biol 5, 140–147 (1998). https://doi.org/10.1038/nsb0298-140
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