A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi.

@article{Login2010A2P,
  title={A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi.},
  author={F. Login and Markus Fries and Xiao-hui Wang and R. Pickersgill and V. Shevchik},
  journal={Molecular microbiology},
  year={2010},
  volume={76 4},
  pages={
          944-55
        }
}
  • F. Login, Markus Fries, +2 authors V. Shevchik
  • Published 2010
  • Medicine, Biology
  • Molecular microbiology
  • The type II secretion system (T2SS) is widely exploited by proteobacteria to secrete enzymes and toxins involved in bacterial survival and pathogenesis. The outer membrane pore formed by the secretin OutD and the inner membrane protein OutC are two key components of the secretion complex, involved in secretion specificity. Here, we show that the periplasmic regions of OutC and OutD interact directly and map the interaction site of OutC to a 20-residue peptide named OutCsip (secretin interacting… CONTINUE READING

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    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 48 REFERENCES
    Insertion of an outer membrane protein in Escherichia coli requires a chaperone‐like protein.
    218
    The underlying mechanisms of type II protein secretion.
    270
    Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae.
    63