Structure and molecular assignment of lactococcal phage TP901-1 baseplate.

@article{Bebeacua2010StructureAM,
  title={Structure and molecular assignment of lactococcal phage TP901-1 baseplate.},
  author={Cecilia Bebeacua and Patrick Bron and Livia Pui Shuen Lai and Christina Skovgaard Vegge and Lone Br{\o}ndsted and Silvia L Spinelli and Val{\'e}rie Campanacci and David Veesler and Marin van Heel and Christian Cambillau},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 50},
  pages={
          39079-86
        }
}
P335 lactococcal phages infect the gram(+) bacterium Lactococcus lactis using a large multiprotein complex located at the distal part of the tail and termed baseplate (BP). The BP harbors the receptor-binding proteins (RBPs), which allow the specific recognition of saccharidic receptors localized on the host cell surface. We report here the electron microscopic structure of the phage TP901-1 wild-type BP as well as those of two mutants bppL (-) and bppU(-), lacking BppL (the RBPs) or both… CONTINUE READING
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References

Publications referenced by this paper.
SHOWING 1-2 OF 2 REFERENCES

Lactococcal Phage TP901-1

L. G. Pell, V. Kanelis, L. W. Donaldson, P. L. Howell, Davidson
  • Baseplate DECEMBER 10,
  • 2010
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

Lactococcal Phage TP901-1 Baseplate 39086 JOURNAL OF BIOLOGICAL CHEMISTRY

P. Chacón, W. Wriggers
  • J. Mol. Biol
  • 2002
VIEW 1 EXCERPT