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Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD

  1. Author:
    Yang, F.
    Forrer, P.
    Dauter, Z.
    Conway, J. F.
    Cheng, N. Q.
    Cerritelli, M. E.
    Steven, A. C.
    Pluckthun, A.
    Wlodawer, A.

  2. Author Address

    Pluckthun A Univ Zurich, Inst Biochem Winterthurerstr 190 CH-8057 Zurich Switzerland Univ Zurich, Inst Biochem CH-8057 Zurich Switzerland NCI, Macromol Crystallog Lab, Program Struct Biol, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA Brookhaven Natl Lab, NCI, FCRDC Upton, NY 11973 USA Brookhaven Natl Lab, NSLS Upton, NY 11973 USA NIAMSD, Struct Biol Lab Bethesda, MD 20892 USA
    1. Year: 2000
  2. Journal: Nature Structural Biology
    1. 7
    2. 3
    3. Pages: 230-237
  4. Type of Article: Article
  1. Abstract:

    The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage lambda, was solved at 1.1 Angstrom resolution. Data were obtained from twinned crystals in space group PZ, and refined with anisotropic temperature factors to an R-factor of 0.098 (R-free = 0.132). GpD (109 residues) has a novel fold with an unusually low content of regular secondary structure. Noncrystallographic trimers with substantial intersubunit interfaces were observed. The C-termini are well ordered and located on one side of the trimer, relatively far from its three-fold axis. The N-termini are disordered up to Ser 15, which is close to the three-fold axis and on the same side as the C-termini. A density map of the icosahedral viral capsid at 15 Angstrom resolution, obtained by cryo-electron microscopy and image reconstruction, reveals gpD trimers, seemingly indistinguishable from the ones seen in the crystals, at all threefold sites. The map further reveals that the side of the trimer that binds to the capsid is the side on which both termini reside. Despite this orientation of the gpD trimer, fusion proteins connected by linker peptides to either terminus bind to the capsid, allowing protein and peptide display. [References: 54]

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