PMID:11034289

Citation	Saint, N, El Hamel, C, Dé, E and Molle, G (2000) Ion channel formation by N-terminal domain: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli. FEMS Microbiol. Lett. 190:261-5
Abstract	The proteolytic fragments of OprFs of Pseudomonas aeruginosa and Pseudomonas fluorescens were identified, respectively, as the first 175 and 177 amino acids from the N-terminal domain. They induced ion channels after reincorporation into planar lipid bilayers (85 and 75 pS, respectively, in 1 M NaCl). A similar conductance value (72 pS) was found for the eight beta-strand OmpA N-terminal domain (OmpA171) of Escherichia coli. We conclude that the N-terminal domain of OprFs is sufficient to induce ion channels and the comparison with OmpA171, provides strong evidence of the existence of an eight-stranded beta-barrel in the N-terminal domain of OprFs.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Ion Channels/metabolism; Lipid Bilayers; Molecular Sequence Data; Porins/chemistry; Porins/genetics; Porins/metabolism; Pseudomonas/genetics; Pseudomonas/metabolism; Pseudomonas aeruginosa/genetics; Pseudomonas aeruginosa/metabolism; Pseudomonas fluorescens/genetics; Pseudomonas fluorescens/metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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