Download MendeleyCrystal Structure of Omp32, the Anion-Selective Porin from Comamonas Acidovorans, in Complex with a Periplasmic Peptideat 2.1 A Resolution
Zeth, K., Diederichs, K., Welte, W., Engelhardt, H.(2000) Structure 8: 981
- PubMed: 10986465
- DOI: https://doi.org/10.1016/s0969-2126(00)00189-1
- Primary Citation of Related Structures:
1E54 - PubMed Abstract:
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.
Organizational Affiliation:
Max-Planck-Institut für Biochemie, Abteilung Molekulare Strukturbiologie, Am Klopferspitz 18a, D-82152, Martinsried, Germany.
