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The OprF membrane domain Family [Function: Structural] Seed alignment | Full alignment | Pfam page | TC-DB page

This family includes homologs to the OprF of Pseudomonas aeruginosa. Members of this family (similar to members of the OmpA family) show a modular architecture, composed of two distinct Structural domains: an N-terminal ß-barrel domain with short turns at the periplasmic ends and long flexible loops at the external ends that anchor the protein to the outer membrane; and a C-terminal domain that protrudes into the periplasmic space interacting with peptidoglycans. The C-terminal domain (named OmpA-like domain), is also found in a number of outer membrane lipoproteins, therefore it is not characteristic of ß-barrels. There is also a distant homology to members of the OmpW family. A recently solved structure reveals a barrel with 8 ß strands.

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Literature references

Alternative folding pathways of the major porin OprF of Pseudomonas aeruginosa
FEBS J. 2012 Mar;279(6):910-8. doi: 10.1111/j.1742-4658.2012.08481.x. Epub 2012 Feb 10.
PMID: 22240095

Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries
mBio. 2011 Dec 6;2(6):e00246-11. doi: 10.1128/mBio.00246-11. Print 2011.
PMID: 22147293

Involvement of the C-terminal part of Pseudomonas fluorescens OprF in the modulation of its pore-forming properties
Biochim Biophys Acta. 2000 Dec 20;1509(1-2):237-44. doi: 10.1016/s0005-2736(00)00300-x.
PMID: 11118535

Ion channel formation by N-terminal domain: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli
FEMS Microbiol Lett. 2000 Sep 15;190(2):261-5. doi: 10.1111/j.1574-6968.2000.tb09296.x.
PMID: 11034289

The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: correlation with a three-dimensional model
J Bacteriol. 2000 Sep;182(18):5251-5. doi: 10.1128/jb.182.18.5251-5255.2000.
PMID: 10960112

Proteins in this family with 3D-structure
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