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Journal of Bacteriology, September 2000, p. 5251-5255, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
The Amino Terminus of Pseudomonas aeruginosa
Outer Membrane Protein OprF Forms Channels in Lipid Bilayer Membranes:
Correlation with a Three-Dimensional Model
Fiona S. L.
Brinkman,
Manjeet
Bains, and
Robert E. W.
Hancock*
Department of Microbiology and Immunology, University of
British Columbia, Vancouver, British Columbia, Canada V6T 1Z3
Received 9 March 2000/Accepted 18 May 2000
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 the larger, channels in lipid bilayers.
Circular dichroism spectroscopy indicated that this protein folds into
a
-sheet-rich structure, and three-dimensional comparative modeling
revealed that it shares significant structural similarity with the
amino terminus of the orthologous protein Escherichia coli
OmpA, which has been shown to form a
-barrel. OprF and OmpA share
only 15% identity in this domain, yet these results support the
utility of modeling such widely divergent
-barrel domains in three
dimensions in order to reveal similarities not readily apparent through
primary sequence comparisons. The model is used to further hypothesize
why porin activity differs for the N-terminal domains of OprF and OmpA.
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, 300-6174 University Blvd., University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3. Phone:
(604) 822-2682. Fax: (604) 822-6041. E-mail:
bob{at}cmdr.ubc.ca.
Journal of Bacteriology, September 2000, p. 5251-5255, Vol. 182, No. 18
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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