Mutational analysis of putative helix-helix interacting GxxxG-motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G.

@article{Oppegrd2008MutationalAO,
  title={Mutational analysis of putative helix-helix interacting GxxxG-motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G.},
  author={Camilla Oppeg{\aa}rd and Juliane S Schmidt and Per Eugen Kristiansen and Jon Nissen-Meyer},
  journal={Biochemistry},
  year={2008},
  volume={47 18},
  pages={5242-9}
}
The membrane-permeabilizing two-peptide bacteriocin lactococcin G consists of two different peptides, LcnG-alpha and LcnG-beta. The bacteriocin contains several tryptophan and tyrosine residues and three putative helix-helix interacting GxxxG-motifs, G 7xxxG 11 and G 18xxxG 22 in LcnG-alpha and G 18xxxG 22 in LcnG-beta. The tryptophan and tyrosine residues and residues in the GxxxG-motifs were altered by site-directed mutagenesis to analyze the structure and membrane-orientation of lactococcin… CONTINUE READING

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Analysis of the two-peptide bacteriocins lactococcin G and enterocin 1071 by site-directed mutagenesis

  • C. Oppegård, G. Fimland, L. Thorbæk, J. Nissen-Meyer
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