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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 beta -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 beta -barrel. OprF and OmpA share only 15% identity in this domain, yet these results support the utility of modeling such widely divergent beta -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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