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

Research output: Contribution to journalArticle

53 Citations (Scopus)

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.

LanguageEnglish
Pages5251-5255
Number of pages5
JournalJournal of bacteriology
Volume182
Issue number18
DOIs
Publication statusPublished - 28 Sep 2000

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

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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.",
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The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes : Correlation with a three-dimensional model. / Brinkman, F. S.L.; Bains, M.; Hancock, Robert.

In: Journal of bacteriology, Vol. 182, No. 18, 28.09.2000, p. 5251-5255.

Research output: Contribution to journalArticle

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