The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: Correlation with a three-dimensional model

F. S.L. Brinkman, M. Bains, Robert Hancock

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Abstract

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

Original languageEnglish
Pages (from-to)5251-5255
Number of pages5
JournalJournal of bacteriology
Volume182
Issue number18
DOIs
Publication statusPublished - 28 Sep 2000
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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