Effects of pore mutations and permeant ion concentration on the spontaneous gating activity of OmpC porin.

@article{Liu2000EffectsOP,
  title={Effects of pore mutations and permeant ion concentration on the spontaneous gating activity of OmpC porin.},
  author={Naili Liu and Hrissi Samartzidou and Keon Woo Lee and James M. Briggs and Anne H. Delcour},
  journal={Protein engineering},
  year={2000},
  volume={13 7},
  pages={491-500}
}
Porins are trimers of beta-barrels that form channels for ions and other hydrophilic solutes in the outer membrane of Gram-negative bacteria. The X-ray structures of OmpF and PhoE show that each monomeric pore is constricted by an extracellular loop that folds into the channel vestibule, a motif that is highly conserved among bacterial porins. Electrostatic calculations have suggested that the distribution of ionizable groups at the constriction zone (or eyelet) may establish an intrinsic… CONTINUE READING