ArticleNature communications2025
Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
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Who cites it
3 citing papers in PubMed.
- Structural mechanisms of pump assembly and drug transport in the AcrAB-TolC efflux system.eLife · 2026Article
- Berberine hydrochloride combination therapy and efflux pump regulation mechanism ameliorates antimicrobial resistance ofMicrobiology spectrum · 2026Article
- Emergence of a multidrug-resistantFrontiers in cellular and infection microbiology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Recent emergence and dissemination of plasmid-borne tmexCD1-toprJ1 tigecycline resistance threatens the efficacy of tigecycline as a "last-resort" defense against bacterial infections. Here, we report two cryo-EM structures of TMexCD1-TOprJ1 alone and in complex with its NMP inhibitor, and both are determined at the resolutions of 2.97 Å and 3.0 Å, respectively. The symmetry of overall architecture explains how the tripartite organization adopts a 3:6:3 protomer stoichiometry (TOprJ1: TMexC1: TMexD1) to assemble an elongated, rod-like pump spanning bacterial double membranes. The periplasmic TMexC1 adaptor bind the trimeric TOprJ1 funnel via a universal "tip-to-tip" contact, and bridges the bottom TMexD1 engine by extensive interactions. A unique form of resting (R) states is observed for TMexD1 trimer. Besides two binding-interfaces of TMexC1 with TOprJ1 and TMexD1, we characterize a substrate/inhibitor-loading cavity. Collectively, these findings constitute molecular bases for assembly and inhibition of transferable TMexCD1-TOprJ1 machinery, and benefit developing next-generation of antimicrobials targeting functional efflux pump.
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Registered trials
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