Outer-membrane protein PhoE from Escherichia coli forms anion-selective pores in lipid-bilayer membranes.
Porin PhoE of the outer membrane of Escherichia coli was isolated and purified. Reconstitution experiments with lipid bilayer membranes showed that this protein formed pores which had a single channel conductance of 210 pS at 0.1 M KCl. The PhoE pores were obviously not voltage-controlled or regulated. In contrast to pores formed by the OmpF porin from E. coli the PhoE channel was found to be anion-selective at neutral pH. Chloride is about three to ten times more permeable through the pore than alkali ions. On the basis of the observed pH dependence of the permeability ratio of anions and cations, this anionic selectivity is explained by the assumption that the PhoE pore contains an excess of fixed positive charges.
D000838:Anions / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D004553:Electric Conductivity; D004563:Electrochemistry; D004926:Escherichia coli / Q000378:metabolism*; D007473:Ion Channels / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000378:metabolism*; D013696:Temperature
D000838:Anions; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins