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

Nature Structural Biology volume 5, pages 140–147 (1998)Cite this article

Abstract

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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Authors and Affiliations

  1. Macromolecular Structure Laboratory, ABL-Basic Research Program, NCI-FCRDC, P.O. Box B, Frederick, Maryland, 21702, USA

    Jacek Lubkowski & Alexander Wlodawer

  2. Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, CH-8057, Zürich, Switzerland

    Frank Hennecke & Andreas Plückthun

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  1. Jacek Lubkowski
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  2. Frank Hennecke
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  3. Andreas Plückthun
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Correspondence to Alexander Wlodawer.

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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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