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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.

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
Citak, F., I. Ghai, F. Rosenkötter, L. Benier, M. Winterhalter, and R. Wagner. (2018). Probing transport of fosfomycin through substrate specific OprO and OprP from Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 495: 1454-1460. 29198700
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.
Lapierre, J. and J.S. Hub. (2023). Converging PMF Calculations of Antibiotic Permeation across an Outer Membrane Porin with Subkilocalorie per Mole Accuracy. J Chem Inf Model 63: 5319-5330. 37560945
Modi, N., I. Bárcena-Uribarri, M. Bains, R. Benz, R.E. Hancock, and U. Kleinekathöfer. (2013). Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: effects of charge and solvation. Biochemistry 52: 5522-5532. 23875754
Modi, N., I. Bárcena-Uribarri, M. Bains, R. Benz, R.E. Hancock, and U. Kleinekathöfer. (2015). Tuning the affinity of anion binding sites in porin channels with negatively charged residues: molecular details for OprP. ACS Chem Biol 10: 441-451. 25333751
Modi, N., S. Ganguly, I. Bárcena-Uribarri, R. Benz, B. van den Berg, and U. Kleinekathöfer. (2015). Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa. Biophys. J. 109: 1429-1438. 26445443
Nikaido, H. (1992). Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6: 435-442. 1373213
Niramitranon, J., M.S. Sansom, and P. Pongprayoon. (2016). Why do the outer membrane proteins OmpF from E. coli and OprP from P. aeruginosa prefer trimer? Simulation studies. J Mol Graph Model 65: 1-7. [Epub: Ahead of Print] 26895142
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