Open AccessIon channel formation by N‐terminal domain: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli
Author(s) -
Saint Nathalie,
El Hamel Chahrazed,
Dé Emmanuelle,
Molle Gérard
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09296.x
Subject(s) - escherichia coli , pseudomonas fluorescens , ion channel , pseudomonas aeruginosa , bacterial outer membrane , chemistry , c terminus , domain (mathematical analysis) , biology , amino acid , biophysics , biochemistry , bacteria , genetics , gene , mathematical analysis , receptor , mathematics
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 β‐strand OmpA N‐terminal domain (OmpA 171 ) of Escherichia coli . We conclude that the N‐terminal domain of OprFs is sufficient to induce ion channels and the comparison with OmpA 171 , provides strong evidence of the existence of an eight‐stranded β‐barrel in the N‐terminal domain of OprFs.