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1.B.5 The Pseudomonas OprP Porin (POP) Family

Two Pseudomonas outer membrane porin proteins, both functionally characterized, comprise the POP family. These porins are anion-selective and transport either phosphate (OprP) or pyrophosphate (OprO) as their physiological substrate.

This family belongs to the: Porin Superfamily I.

References associated with 1.B.5 family:

Benz, R., C. Egli, and R.E. Hancock. (1993). 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. 1149: 224-230. 8323941
Hancock, R.E., C. Egli, R. Benz, and R.J. Siehnel. (1992). Overexpression in Escherichia coli and functional analysis of a novel PPi-selective porin, oprO, from Pseudomonas aeruginosa. J. Bacteriol. 174: 471-476. 1370289
Hancock, R.E.W., R. Siehnel and N. Martin (1990). Outer membrane proteins of Pseudomonas. Mol. Microbiol. 4: 1069-1075. 1700255
Jeanteur, D., J.H. Lakey and F. Pattus (1991). The bacterial porin superfamily: sequence alignment and structure prediction. Mol. Microbiol. 5: 2153-2164. 1662760
Jeanteur, D., J.H. Lakey and F. Pattus (1994). The porin superfamily: diversity and common features. In: Bacterial Cell Wall. Edited by Ghuysen, J.M., Hakenbeck, R. Elsevier, Amsterdam, pp. 363-380.
Nikaido, H. (1992). Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6: 435-442. 1373213
Rehm, B.H., G. Boheim, J. Tommassen, and U.K. Winkler. (1994). Overexpression of algE in Escherichia coli: subcellular localization, purification, and ion channel properties. J. Bacteriol. 176: 5639-5647. 7521870
Schulz, G.E. (1996). Porins: general to specific, native to engineered passive pores. Curr. Opin. Struc. Biol. 6: 485-490. 8794162
Siehnel, R., N.L. Martin and R.E.W. Hancock (1990). Sequence and relatedness in other bacteria of the Pseudomonas aeruginosa oprP gene coding for the phosphate-specific porin P. Mol. Microbiol. 4: 831-838. 1697017