Porin isolated from the cell envelope of Rhodopseudomonas capsulata.
The isolate major outer membrane protein from Rhodopseudomonas capsulata St. Louis (ATCC 23782) has a high porin activity in reconstituted phospholipid liposomes. The pore size of the homooligomeric porin with subunits of Mr 33,000 was determined to be about 0.8 nm in radius. Circular dichroism data revealed major portions of the beta structure. Heating of the oligomer resulted in monomer formation, loss of porin activity (60 to 70 degrees C), and change to alpha structure (100 degrees C).
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002462:Cell Membrane / Q000032:analysis; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000032:analysis / Q000302:isolation & purification*; D008970:Molecular Weight; D018272:Porins; D011487:Protein Conformation; D012241:Rhodopseudomonas / Q000032:analysis*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008565:Membrane Proteins; D018272:Porins