|Browse||Text search||Protein search||Domain search||Download||User manual||Related links||Citation & Contact|
This is a small family named after the porin fomA found n the outer membrane of Fusobacterium nucleatum. FomA is a trimeric protein, which exhibits channel properties similar to that of the other general porins. Deletions in the largest proposed external region (loop L6), made the fomA porins considerably more permeable to antibiotics, indicating larger pore channels. Results obtained from limited proteolysis of purified fomA, indicate that the N-terminal part of the protein is not an integral part of the ß-barrel, but forms a periplasmic domain instead, therefore the protein is proposed to form the ß-barrel distinct from the periplasmic N-terminal domain.
Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins
Microbiology (Reading). 2002 Nov;148(Pt 11):3395-3403. doi: 10.1099/00221287-148-11-3395.
Topological investigations of the FomA porin from Fusobacterium nucleatum and identification of the constriction loop L6
Microbiology (Reading). 2001 Apr;147(Pt 4):1059-1067. doi: 10.1099/00221287-147-4-1059.