Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1
Article Abstract:
The complex formation between porin and porin-associated protein (PAP) of the gram-negative bacteria Rhodospirillum rubrum FR1 stabilizes the outer membrane. The stability is due to increase in the stability of porin and membrane peptidoglycan binding. The complex contains porin in the trimeric form and has a beta-sheet structure. PAP has no channel forming activity as the membrane conductance of the porin-PAP complex is similar to the porin channels. The binding of PAP to porin requires divalent cations.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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Immunochemical structure of the OmpD porin from Salmonella typhimurium
Article Abstract:
The structure of Salmonella typhimurium SH 7454 OmpD porin was analyzed by utilizing cyanogen bromide digestion and subsequent amino acid sequencing of the protein fragments. The OmpD porin of Salmonella typhimurium strain SH 7454 is composed of 96 protein residues and exhibits an amino acid sequence that is 75% similar to the NmpC, Lc and OmpC porins of Escherichia coli. Furthermore, the OmpD porin is 68% homologous to the OmpC porin of Salmonella typhimurium.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Lipopolysaccharide and porin of Roseobacter denitrificans, confirming its phylogenetic relationship to the alpha-3 subgroup of proteobacteria
Article Abstract:
Treatment of the major porin of Roseobacter denitrificans with EDTA causes dissociation of the oligomers into monomers. The 12 N-terminal amino acids of the monomers display sequence homology with the porins of Rhodobacter (R)capsulatus, R. spheroids and Rhodopseudomonas blastica. On the basis of these characteristics, Roseobacter dentrificans might be renamed Rhodobacter dentrificans.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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