Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution.

@article{Zeth2000CrystalSO,
  title={Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution.},
  author={Kornelius Zeth and Kay Diederichs and Wolfram Welte and Harald Engelhardt},
  journal={Structure},
  year={2000},
  volume={8 9},
  pages={981-92}
}
BACKGROUND Porins provide diffusion channels for salts and small organic molecules in the outer membrane of bacteria. In OmpF from Escherichia coli and related porins, an electrostatic field across the channel and a potential, originating from a surplus of negative charges, create moderate cation selectivity. Here, we investigate the strongly anion-selective porin Omp32 from Comamonas acidovorans, which is closely homologous to the porins of pathogenic Bordetella and Neisseria species… CONTINUE READING

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