The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: Correlation with a three-dimensional model
Fsl. Brinkman et al., The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: Correlation with a three-dimensional model, J BACT, 182(18), 2000, pp. 5251-5255
Pseudomonas aeruginosa OprF forms 0.36-nS channels and, rarely, 2- to 5-nS
channels in lipid bilayer membranes. We show that a protein comprising only
the N-terminal 162-amino-acid domain of OprF formed the smaller, but not t
he larger, channels in lipid bilayers. Circular dichroism spectroscopy indi
cated that this protein folds into a beta-sheet-rich structure, and three-d
imensional comparative modeling revealed that it shares significant structu
ral similarity with the amino terminus of the orthologous protein Escherich
ia coli OmpA, which has been shown to form a beta-barrel. OprF and OmpA sha
re only 15% identity in this domain, yet these results support the utility
of modeling such widely divergent beta-barrel domains in three dimensions i
n order to reveal similarities not readily apparent through primary sequenc
e comparisons. The model is used to further hypothesize why porin activity
differs for the N-terminal domains of OprF and OmpA.