ArticleBiochemistry2012
OccK channels from Pseudomonas aeruginosa exhibit diverse single-channel electrical signatures but conserved anion selectivity.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Understanding Drug Permeability inLife (Basel, Switzerland) · 2025Review
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Current noise of a protein-selective biological nanopore.Proteomics · 2022Article
- Role of internal loop dynamics in antibiotic permeability of outer membrane porins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Towards understanding single-channel characteristics of OccK8 purified from Pseudomonas aeruginosa.European biophysics journal : EBJ · 2021Article
- OMPdb: A Global Hub of Beta-Barrel Outer Membrane Proteins.Frontiers in bioinformatics · 2021Article
- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- Mechanisms of intrinsic resistance and acquired susceptibility of Pseudomonas aeruginosa isolated from cystic fibrosis patients to temocillin, a revived antibiotic.Scientific reports · 2017Article
- Exploring bacterial outer membrane barrier to combat bad bugs.Infection and drug resistance · 2017Review
- The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.ACS chemical biology · 2016Article
- In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.International journal of molecular sciences · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
- The OpdQ porin of Pseudomonas aeruginosa is regulated by environmental signals associated with cystic fibrosis including nitrate-induced regulation involving the NarXL two-component system.MicrobiologyOpen · 2015Article
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Biomedical diagnosis perspective of epigenetic detections using alpha-hemolysin nanopore.AIMS materials science · 2015Article
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
- Toward understanding the outer membrane uptake of small molecules by Pseudomonas aeruginosa.The Journal of biological chemistry · 2013Article
- Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?Biochimica et biophysica acta · 2013Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Cation selectivity is a conserved feature in the OccD subfamily of Pseudomonas aeruginosa.Biochimica et biophysica acta · 2012Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa is a Gram-negative bacterium that utilizes substrate-specific outer membrane (OM) proteins for the uptake of small, water-soluble nutrients employed in the growth and function of the cell. In this paper, we present for the first time a comprehensive single-channel examination of seven members of the OM carboxylate channel K (OccK) subfamily. Recent biochemical, functional, and structural characterization of the OccK proteins revealed their common features, such as a closely related, monomeric, 18-stranded β-barrel conformation with a kidney-shaped transmembrane pore and the presence of a basic ladder within the channel lumen. Here, we report that the OccK proteins exhibited fairly distinct unitary conductance values, in a much broader range than previously expected, which includes low (~40-100 pS) and medium (~100-380 pS) conductance. These proteins showed diverse single-channel dynamics of current gating transitions, revealing one-open substate (OccK3), two-open substate (OccK4-OccK6), and three-open substate (OccK1, OccK2, and OccK7) kinetics with functionally distinct conformations. Interestingly, we discovered that anion selectivity is a conserved trait among the members of the OccK subfamily, confirming the presence of a net pool of positively charged residues within their central constriction. Moreover, these results are in accord with an increased specificity and selectivity of these protein channels for negatively charged, carboxylate-containing substrates. Our findings might ignite future functional examinations and full atomistic computational studies for unraveling a mechanistic understanding of the passage of small molecules across the lumen of substrate-specific, β-barrel OM proteins.
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