Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP: Effects of charge and solvation

Niraj Modi, Iván Bárcena-Uribarri, Manjeet Bains, Roland Benz, Robert Hancock, Ulrich Kleinekathöfer

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The outer membrane porin OprP of Pseudomonas aeruginosa forms a highly specific phosphate selective channel. This channel is responsible for the high-affinity uptake of phosphate ions into the periplasmic space of the bacteria. A detailed investigation of the structure-function relationship of OprP is inevitable to decipher the anion and phosphate selectivity of this porin in particular and to broaden the present understanding of the ion selectivity of different channels. To this end we investigated the role of the central arginine of OprP, R133, in terms of its effects in selectivity and ion transport properties of the pore. Electrophysiological bilayer measurements and free-energy molecular dynamics simulations were carried out to probe the transport of different ions through various R133 mutants. For these mutants, the change in phosphate binding specificity, ion conduction, and anion selectivity was determined and compared to previous molecular dynamic calculations and electrophysiological measurements with wild-type OprP. Molecular analysis revealed a rather particular role of arginine 133 and its charge, while at the same time this residue together with the network of other residues, namely, D94 and Y114, has the ability to dehydrate the permeating ion. These very specific features govern the ion selectivity of OprP.

LanguageEnglish
Pages5522-5532
Number of pages11
JournalBiochemistry
Volume52
Issue number33
DOIs
Publication statusPublished - 20 Aug 2013

ASJC Scopus subject areas

  • Biochemistry

Cite this

Modi, Niraj ; Bárcena-Uribarri, Iván ; Bains, Manjeet ; Benz, Roland ; Hancock, Robert ; Kleinekathöfer, Ulrich. / Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP : Effects of charge and solvation. In: Biochemistry. 2013 ; Vol. 52, No. 33. pp. 5522-5532.
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abstract = "The outer membrane porin OprP of Pseudomonas aeruginosa forms a highly specific phosphate selective channel. This channel is responsible for the high-affinity uptake of phosphate ions into the periplasmic space of the bacteria. A detailed investigation of the structure-function relationship of OprP is inevitable to decipher the anion and phosphate selectivity of this porin in particular and to broaden the present understanding of the ion selectivity of different channels. To this end we investigated the role of the central arginine of OprP, R133, in terms of its effects in selectivity and ion transport properties of the pore. Electrophysiological bilayer measurements and free-energy molecular dynamics simulations were carried out to probe the transport of different ions through various R133 mutants. For these mutants, the change in phosphate binding specificity, ion conduction, and anion selectivity was determined and compared to previous molecular dynamic calculations and electrophysiological measurements with wild-type OprP. Molecular analysis revealed a rather particular role of arginine 133 and its charge, while at the same time this residue together with the network of other residues, namely, D94 and Y114, has the ability to dehydrate the permeating ion. These very specific features govern the ion selectivity of OprP.",
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Role of the central arginine R133 toward the ion selectivity of the phosphate specific channel OprP : Effects of charge and solvation. / Modi, Niraj; Bárcena-Uribarri, Iván; Bains, Manjeet; Benz, Roland; Hancock, Robert; Kleinekathöfer, Ulrich.

In: Biochemistry, Vol. 52, No. 33, 20.08.2013, p. 5522-5532.

Research output: Contribution to journalArticle

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T2 - Biochemistry

AU - Modi, Niraj

AU - Bárcena-Uribarri, Iván

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AU - Hancock, Robert

AU - Kleinekathöfer, Ulrich

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AB - The outer membrane porin OprP of Pseudomonas aeruginosa forms a highly specific phosphate selective channel. This channel is responsible for the high-affinity uptake of phosphate ions into the periplasmic space of the bacteria. A detailed investigation of the structure-function relationship of OprP is inevitable to decipher the anion and phosphate selectivity of this porin in particular and to broaden the present understanding of the ion selectivity of different channels. To this end we investigated the role of the central arginine of OprP, R133, in terms of its effects in selectivity and ion transport properties of the pore. Electrophysiological bilayer measurements and free-energy molecular dynamics simulations were carried out to probe the transport of different ions through various R133 mutants. For these mutants, the change in phosphate binding specificity, ion conduction, and anion selectivity was determined and compared to previous molecular dynamic calculations and electrophysiological measurements with wild-type OprP. Molecular analysis revealed a rather particular role of arginine 133 and its charge, while at the same time this residue together with the network of other residues, namely, D94 and Y114, has the ability to dehydrate the permeating ion. These very specific features govern the ion selectivity of OprP.

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