ArticleNature communications2019
Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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82 citing papers in PubMed, 67 citations in OpenAlex.
- High resolution cryo-EM structure of theJournal of structural biology: X · 2026Article
- Structural insights into a substrate translocation pathway revealed by the RND efflux pump complex MexJK fromScience advances · 2026Article
- Efflux-mediated carbapenem resistance: unveiling genetic drivers, clinical implications, and strategies for global antimicrobial stewardship.Antonie van Leeuwenhoek · 2026Review
- Comparison of the expression of small regulatory RNAs AS1974, AS2779, IGR2780 and the Hfq gene in carbapenem-resistant and susceptible clinical isolates of Pseudomonas aeruginosa.BMC microbiology · 2026Article
- Structure of chloramphenicol-bound MexB reveals residues in the distal binding pocket that are critical for substrate recognition.Journal of biochemistry · 2026Article
- Hospital-Associated Antimicrobial Resistant Bacteria on 95 Mobile Phones: An International Metagenomic "Phonome" Analysis.MicrobiologyOpen · 2026Article
- Secretin-interacting plug proteins prevent antibiotic influx during type IV pilus assembly in Pseudomonas aeruginosa.Nature communications · 2026Article
- Medicinal Plants: A Promising Therapeutic Approach for Addressing Antimicrobial Resistance.International journal of molecular sciences · 2026Review
- A lipoprotein partner for theeLife · 2026Article
- A missing link for efflux pumps.eLife · 2026Article
- Role of hydrogen sulfide in bacterial antibiotic tolerance: from mechanisms to therapeutic targeting.Frontiers in cellular and infection microbiology · 2026Review
- RND efflux pump inhibitor-like natural products as antibiotic adjuvants against multidrug-resistant gram-negative bacteria: a graded-evidence review.Frontiers in microbiology · 2026Review
- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Alanine Scanning Analysis of MexB in Multidrug-Resistant Pseudomonas aeruginosa Using the Native Type I-F CRISPR-Cas-Mediated Genome Editing.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Conformational plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity.Nature communications · 2025Article
- Artificial intelligence in protein-based detection and inhibition of AMR pathways.Journal of computer-aided molecular design · 2025Review
- Evaluating the ciprofloxacin potentiation efficacy of repurposed drug flupentixol through efflux pump inhibition of pathogenic bacteria.Scientific reports · 2025Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Colistin resistance in the era of antimicrobial resistance: challenges and strategic countermeasures.Folia microbiologica · 2025Review
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
22 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Pseudomonas aeruginosa, MexAB-OprM plays a central role in multidrug resistance by ejecting various drug compounds, which is one of the causes of serious nosocomial infections. Although the structures of the components of MexAB-OprM have been solved individually by X-ray crystallography, no structural information for fully assembled pumps from P. aeruginosa were previously available. In this study, we present the structure of wild-type MexAB-OprM in the presence or absence of drugs at near-atomic resolution. The structure reveals that OprM does not interact with MexB directly, and that it opens its periplasmic gate by forming a complex. Furthermore, we confirm the residues essential for complex formation and observed a movement of the drug entrance gate. Based on these results, we propose mechanisms for complex formation and drug efflux.
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