ArticleCommunications biology2023
Structure of anhydrotetracycline-bound Tet(X6) reveals the mechanism for inhibition of type 1 tetracycline destructases.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 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.
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Who cites it
9 citing papers in PubMed.
- Evolution, Mechanisms, and Therapeutic Implications of Mobile Tetracycline Destructases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Threat and Control ofFoods (Basel, Switzerland) · 2025Review
- Covalent Irreversible Inhibitors of Tetracycline Destructases.ACS infectious diseases · 2025Article
- Binding assays enable discovery of Tet(X) inhibitors that combat tetracycline destructase resistance.Chemical science · 2025Article
- Emergence of transferable tigecycline and eravacycline resistance gene tet(X4) in Escherichia coli isolates from Iran.Scientific reports · 2025Article
- C10-Benzoate Esters of Anhydrotetracycline Inhibit Tetracycline Destructases and Recover Tetracycline Antibacterial Activity.ACS infectious diseases · 2025Article
- Sequence-structure-function characterization of the emerging tetracycline destructase family of antibiotic resistance enzymes.Communications biology · 2024Article
- A promising metabolite, 9-aminominocycline, restores the sensitivity of tigecycline againstFrontiers in microbiology · 2024Article
- Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.Acta crystallographica. Section F, Structural biology communications · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors.
Funding
Abstract
Inactivation of tetracycline antibiotics by tetracycline destructases (TDases) remains a clinical and agricultural threat. TDases can be classified as type 1 Tet(X)-like TDases and type 2 soil-derived TDases. Type 1 TDases are widely identified in clinical pathogens. A combination therapy of tetracycline and a TDase inhibitor is much needed to rescue the clinical efficacy of tetracyclines. Anhydrotetracycline is a pan-TDase inhibitor that inhibits both type 1 and type 2 TDases. Here, we present structural, biochemical, and phenotypic evidence that anhydrotetracycline binds in a substrate-like orientation and competitively inhibits the type 1 TDase Tet(X6) to rescue tetracycline antibiotic activity as a sacrificial substrate. Anhydrotetracycline interacting residues of Tet(X6) are conserved within type 1 TDases, indicating a conserved binding mode and mechanism of inhibition. This mode of binding and inhibition is distinct from anhydrotetracycline's inhibition of type 2 TDases. This study forms the framework for development of next-generation therapies to counteract enzymatic tetracycline resistance.
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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.