ArticleNature communications2024
Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and β-lactam antibiotic resistance.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Regulation of PBP2x Surface Localization byPathogens (Basel, Switzerland) · 2026Article
- Optimized bacterial expression of a synthetic BRIL antibody.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Periplasmic crowding and peptidoglycan hydrolase activity as drivers of outer membrane vesiculation in Acinetobacter baumannii.Communications biology · 2026Article
- From the lens of early-career researchers: bridging science, technology, arts, and humanities to tackle antimicrobial resistance.Nature communications · 2026Review
- Design and Optimization of BRIL Fusion Constructs for Membrane Protein Cryo-EM Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance.Nature communications · 2025Article
- Antechodynamics and Antechokinetics: Dynamics and Kinetics of Antibiotic Resistance Biomolecules.Biomolecules · 2025Review
- Bacterial peptidoglycan as a living polymer.Current opinion in chemical biology · 2025Review
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Bacteria invest significant resources into the continuous creation and tailoring of their essential protective peptidoglycan (PG) cell wall. Several soluble PG biosynthesis products in the periplasm are transported to the cytosol for recycling, leading to enhanced bacterial fitness. GlcNAc-1,6-anhydroMurNAc and peptide variants are transported by the essential major facilitator superfamily importer AmpG in Gram-negative pathogens including Escherichia coli, Klebsiella pneumoniae, Acinetobacter baumannii, and Pseudomonas aeruginosa. Accumulation of GlcNAc-1,6-anhydroMurNAc-pentapeptides also results from β-lactam antibiotic induced cell wall damage. In some species, these products upregulate the β-lactamase AmpC, which hydrolyzes β-lactams to allow for bacterial survival and drug-resistant infections. Here, we have used cryo-electron microscopy and chemical synthesis of substrates in an integrated structural, biochemical, and cellular analysis of AmpG. We show how AmpG accommodates the large GlcNAc-1,6-anhydroMurNAc peptides, including a unique hydrophobic vestibule to the substrate binding cavity, and characterize residues involved in binding that inform the mechanism of proton-mediated transport.
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Registered trials
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