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This family is comprised by proteins similar to the phosphate-selective porins O and P, which are found mainly in Pseudomonas aeruginosa. These anion-specific porins possess a binding site that has a higher affinity to phosphate than chloride ions. Porin O (OprO) has a higher affinity to polyphosphates, while porin P (OprP) has a higher affinity to orthophosphate. In Pseudomonas aeruginosa, porin O was found to be expressed only under phosphate-starvation conditions during the stationary growth phase. The crystal structure of OprP has revealed a 16-stranded ß-barrel similar to other general diffusion porins.
Polyphosphate-selective porin OprO of Pseudomonas aeruginosa: expression, purification and sequence
Mol Microbiol. 1992 Aug;6(16):2319-26. doi: 10.1111/j.1365-2958.1992.tb01407.x.
Anion transport through the phosphate-specific OprP-channel of the Pseudomonas aeruginosa outer membrane: effects of phosphate, di- and tribasic anions and of negatively-charged lipids
Biochim Biophys Acta. 1993 Jul 4;1149(2):224-30. doi: 10.1016/0005-2736(93)90205-e.
The bacterial porin superfamily: sequence alignment and structure prediction
Mol Microbiol. 1991 Sep;5(9):2153-64. doi: 10.1111/j.1365-2958.1991.tb02145.x.
An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
Nat Struct Mol Biol. 2007 Jan;14(1):85-7. doi: 10.1038/nsmb1189. Epub 2006 Dec 24.
|Proteins in this family with 3D-structure|