Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.

@article{Hirano2007StructuralSO,
  title={Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.},
  author={Yu Hirano and Md Motarab Hossain and Kazuki Takeda and Hajime Tokuda and Kunio Miki},
  journal={Structure},
  year={2007},
  volume={15 8},
  pages={963-76}
}
NlpE, an outer membrane lipoprotein, functions during envelope stress responses in Gram-negative bacteria. In Escherichia coli, adhesion to abiotic surfaces has been reported to activate the Cpx pathway in an NlpE-dependent manner. External copper ions are also thought to activate the Cpx pathway mediated by NlpE. We determined the crystal structure of NlpE from E. coli at 2.6 A resolution. The structure showed that NlpE consists of two beta barrel domains. The N-terminal domain resembles the… CONTINUE READING
9 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

Similar Papers

Loading similar papers…