ArticleThe Journal of biological chemistry2013
Toward understanding the outer membrane uptake of small molecules by Pseudomonas aeruginosa.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 57 citations in OpenAlex.
- Antibiotic resistance inFrontiers in microbiology · 2026Review
- Understanding Drug Permeability inLife (Basel, Switzerland) · 2025Review
- Attenuated Strains of Pseudomonas aeruginosa: A Promising Cell Factory for Rhamnolipid Production.Microbial biotechnology · 2025Review
- Interplay between porin deficiency, fitness, and virulence in carbapenem-non-susceptible Pseudomonas aeruginosa and Enterobacteriaceae.PLoS pathogens · 2025Review
- From Polymeric Nanoformulations to Polyphenols-Strategies for Enhancing the Efficacy and Drug Delivery of Gentamicin.Antibiotics (Basel, Switzerland) · 2024Review
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Towards understanding single-channel characteristics of OccK8 purified from Pseudomonas aeruginosa.European biophysics journal : EBJ · 2021Article
- Dissociating antibacterial from ototoxic effects of gentamicin C-subtypes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Permeability barriers of Gram-negative pathogens.Annals of the New York Academy of Sciences · 2020Review
- Can Biofilm Be Reversed Through Quorum Sensing inFrontiers in microbiology · 2019Article
- Superoxide dismutase activity confers (p)ppGpp-mediated antibiotic tolerance to stationary-phaseProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Probing the binding affinities of imipenem and ertapenem for outer membrane carboxylate channel D1 (OccD1) from P. aeruginosa: simulation studies.Journal of molecular modeling · 2017Article
- Defining the Roles of the Cation Diffusion Facilitators in FeFrontiers in cellular and infection microbiology · 2017Article
- Article
- Exploring bacterial outer membrane barrier to combat bad bugs.Infection and drug resistance · 2017Review
- Role of the Native Outer-Membrane Environment on the Transporter BtuB.Biophysical journal · 2016Article
- The Transmembrane Domain of a Bicomponent ABC Transporter Exhibits Channel-Forming Activity.ACS chemical biology · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Because small molecules enter Gram-negative bacteria via outer membrane (OM) channels, understanding OM transport is essential for the rational design of improved and new antibiotics. In the human pathogen Pseudomonas aeruginosa, most small molecules are taken up by outer membrane carboxylate channel (Occ) proteins, which can be divided into two distinct subfamilies, OccD and OccK. Here we characterize substrate transport mediated by Occ proteins belonging to both subfamilies. Based on the determination of the OccK2-glucuronate co-crystal structure, we identify the channel residues that are essential for substrate transport. We further show that the pore regions of the channels are rigid in the OccK subfamily and highly dynamic in the OccD subfamily. We also demonstrate that the substrate carboxylate group interacts with central residues of the basic ladder, a row of arginine and lysine residues that leads to and away from the binding site at the channel constriction. Moreover, the importance of the basic ladder residues corresponds to their degree of conservation. Finally, we apply the generated insights by converting the archetype of the entire family, OccD1, from a basic amino acid-specific channel into a channel with a preference for negatively charged amino acids.
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Registered trials
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.