Evidence map›Paper›PMID 26445443›Full record

ArticleBiophysical journal2015

Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa.

Niraj Modi, Sonalli Ganguly, Iván Bárcena-Uribarri, Roland Benz, Bert van den Berg, Ulrich Kleinekathöfer

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Targeting Outer Membrane Vesicles ofJournal of microbiology and biotechnology · 2026
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  3. Understanding Drug Permeability inLife (Basel, Switzerland) · 2025
    Review
  4. Outer membrane permeability ofMicrobiology spectrum · 2025
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  5. Article
  6. Review
  7. Article
  8. Frontiers in cellular and infection microbiology · 2024
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Bacterial Resistance to Antimicrobial Agents.Antibiotics (Basel, Switzerland) · 2021
    Review
  14. Structural insights into the main S-layer unit ofThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Niraj ModiDepartment of Physics and Earth Sciences, Jacobs University Bremen, Bremen, Germany.
Sonalli GangulyDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Iván Bárcena-UribarriDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Roland BenzDepartment of Life Sciences and Chemistry, Jacobs University Bremen, Bremen, Germany.
Bert van den BergInstitute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne, UK. Electronic address: bert.van-den-berg@ncl.ac.uk.
Ulrich KleinekathöferDepartment of Physics and Earth Sciences, Jacobs University Bremen, Bremen, Germany. Electronic address: u.kleinekathoefer@jacobs-university.de.
Constructor University · DENewcastle University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria functions as a selective permeability barrier between cell and environment. For nutrient acquisition, the OM contains a number of channels that mediate uptake of small molecules by diffusion. Many of these channels are specific, i.e., they prefer certain substrates over others. In electrophysiological experiments, the OM channels OprP and OprO from Pseudomonas aeruginosa show a specificity for phosphate and diphosphate, respectively. In this study we use x-ray crystallography, free-energy molecular dynamics (MD) simulations, and electrophysiology to uncover the atomic basis for the different substrate specificity of these highly similar channels. A structural analysis of OprP and OprO revealed two crucial differences in the central constriction region. In OprP there are two tyrosine residues, Y62 and Y114, whereas the corresponding residues in OprO are phenylalanine F62 and aspartate D114. To probe the importance of these two residues in generating the different substrate specificities, the double mutants were generated in silico and in vitro. Applied-field MD simulations and electrophysiological experiments demonstrated that the double mutations interchange the phosphate and diphosphate specificities of OprP and OprO. Our findings outline a possible strategy to rationally design channel specificity by modification of a small number of residues that may be applicable to other pores as well.

Indexed as

Bacterial ProteinsBlotting, WesternCrystallography, X-RayElectrophoresis, Polyacrylamide GelEscherichia coliMembrane PotentialsMembranes, ArtificialMolecular Dynamics SimulationMutationPolyphosphatesPorinsPotassium ChlorideProtein ConformationPseudomonas aeruginosaSubstrate SpecificityBacterial ProteinsMembranes, ArtificialOprO protein, Pseudomonas aeruginosaoprP protein, Pseudomonas aeruginosaPolyphosphatesPorinsPotassium Chloride

Identifiers

PMID26445443
PMCPMC4601001
OpenAlexW2106947904

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.