Subunit structure of functional porin oligomers that form permeability channels in the other membrane of Escherichia coli.
Oligomers of a protein, porin, form permeability channels in the outer membrane of Escherichia coli B. A functional porin oligomer was identified and was purified to homogeneity by gel filtration in the presence of salts and sodium dodecyl sulfate. Molecular weights of purified porin oligomer and heat-dissociated monomer appeared to be 102,900 and 32,600, respectively, when determined by sedimentation equilibrium in the presence of sodium dodecyl sulfate. We concluded that the porin oligomer thus consists of three identical subunits. These data and results from other laboratories suggest porin trimers exist also in the outer membrane of intact cells, and participate in the formation of permeability channels. It was found that porin trimer bound less sodium dodecyl sulfate than the porin monomer.
D001426:Bacterial Proteins / Q000302:isolation & purification; D002462:Cell Membrane / Q000648:ultrastructure*; D002463:Cell Membrane Permeability; D002942:Circular Dichroism; D004926:Escherichia coli / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D011485:Protein Binding; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D008565:Membrane Proteins; D012967:Sodium Dodecyl Sulfate