1E54

Anion-selective porin from Comamonas acidovorans

Summary for 1E54

• Entry DOI: 10.2210/pdb1e54/pdb
• Descriptor: OUTER MEMBRANE PORIN PROTEIN 32, OMP32, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: outer membrane protein, anionen channel, channel protein, beta barrel
• Biological source: COMAMONAS ACIDOVORANS; More
• Total number of polymer chains: 2
• Total formula weight: 35887.61

Authors

Zeth, K.,Diederichs, K.,Welte, W.,Engelhardt, H. (deposition date: 2000-07-17, release date: 2001-07-12, Last modification date: 2024-10-16)

Primary citation

Zeth, K.,Diederichs, K.,Welte, W.,Engelhardt, H.
Crystal Structure of Omp32, the Anion-Selective Porin from Comamonas Acidovorans, in Complex with a Periplasmic Peptideat 2.1 A Resolution
Structure, 8:981-, 2000

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.

PubMed: 10986465
DOI: 10.1016/S0969-2126(00)00189-1

Experimental method

X-RAY DIFFRACTION (2.1 Å)