Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.

@article{Miles2006AssemblyOT,
  title={Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.},
  author={George Miles and Lakmal Jayasinghe and Hagan Bayley},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 4},
  pages={2205-14}
}
Staphylococcal leukocidin (Luk) and alpha-hemolysin (alphaHL) are members of the same family of beta barrel pore-forming toxins (betaPFTs). Although the alphaHL pore is a homoheptamer, the Luk pore is formed by the co-assembly of four copies each of the two distantly related polypeptides, LukF and LukS, to form an octamer. Here, we examine N- and C-terminal truncation mutants of LukF and LukS. LukF subunits missing up to nineteen N-terminal amino acids are capable of producing stable… CONTINUE READING

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