ArticleNature communications2017
Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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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.
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Who cites it
57 citing papers in PubMed.
- Structural insights into a substrate translocation pathway revealed by the RND efflux pump complex MexJK fromScience advances · 2026Article
- Structure of chloramphenicol-bound MexB reveals residues in the distal binding pocket that are critical for substrate recognition.Journal of biochemistry · 2026Article
- Cryo-EM structures of a MexB-MexY chimeric efflux pump reveal that large open clefts are intrinsic to the MexY porter domain.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Article
- Conformational plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity.Nature communications · 2025Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Cryo-EM structure of themBio · 2025Article
- Sharing ofmBio · 2025Article
- Insights into substrate recognition and export tunnel preferences in the efflux transporter AcrB.Protein science : a publication of the Protein Society · 2025Article
- Mutation-based mechanism and evolution of the potent multidrug efflux pump RE-CmeABC inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structures of the mycobacterial MmpL4 and MmpL5 transporters provide insights into their role in siderophore export and iron acquisition.PLoS biology · 2024Article
- Structural analysis of resistance-nodulation cell division transporters.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural basis of DNA recognition of themBio · 2024Article
- Molecular insights into the determinants of substrate specificity and efflux inhibition of the RND efflux pumps AcrB and AdeB.Microbiology (Reading, England) · 2024Review
- Cryo-Electron Microscopy Structures of a Campylobacter Multidrug Efflux Pump Reveal a Novel Mechanism of Drug Recognition and Resistance.Microbiology spectrum · 2023Article
- Crystal structures of multidrug efflux transporters fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Excessive disinfection aggravated the environmental prevalence of antimicrobial resistance during COVID-19 pandemic.The Science of the total environment · 2023Article
- Cancer Drug Delivery Systems Using Bacterial Toxin Translocation Mechanisms.Bioengineering (Basel, Switzerland) · 2023Review
- Article
- AcrAB-TolC, a major efflux pump in Gram negative bacteria: toward understanding its operation mechanism.BMB reports · 2023Review
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Resistance-nodulation-cell division efflux pumps are integral membrane proteins that catalyze the export of substrates across cell membranes. Within the hydrophobe-amphiphile efflux subfamily, these resistance-nodulation-cell division proteins largely form trimeric efflux pumps. The drug efflux process has been proposed to entail a synchronized motion between subunits of the trimer to advance the transport cycle, leading to the extrusion of drug molecules. Here we use X-ray crystallography and single-molecule fluorescence resonance energy transfer imaging to elucidate the structures and functional dynamics of the Campylobacter jejuni CmeB multidrug efflux pump. We find that the CmeB trimer displays a very unique conformation. A direct observation of transport dynamics in individual CmeB trimers embedded in membrane vesicles indicates that each CmeB subunit undergoes conformational transitions uncoordinated and independent of each other. On the basis of our findings and analyses, we propose a model for transport mechanism where CmeB protomers function independently within the trimer.Multidrug efflux pumps significantly contribute for bacteria resistance to antibiotics. Here the authors present the structure of Campylobacter jejuni CmeB pump combined with functional FRET assays to propose a transport mechanism where each CmeB protomers is functionally independent from the trimer.
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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.