ArticleJournal of the American Chemical Society2017
Muropeptide Binding and the X-ray Structure of the Effector Domain of the Transcriptional Regulator AmpR of Pseudomonas aeruginosa.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 42 citations in OpenAlex.
- Non canonical perspectives on AmpR mediated ampC expression in Gram negative bacteria, with particular emphasis on the potential regulatory purview of FtsZ.World journal of microbiology & biotechnology · 2026Review
- Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026Article
- Ring opening, conformational analysis and NagZ inhibition of a GlcNAc-configured iminosugar-derived aziridine.Carbohydrate research · 2026Article
- Article
- Parallel microevolution of multidrug resistance and hypermucoviscosity in two carbapenem-resistant Pseudomonas aeruginosa clinical isolates with strikingly divergent virulence outcomes.BMC microbiology · 2026Article
- Disruption of undecaprenyl phosphate recycling suppresses ampC beta-lactamase induction in Pseudomonas aeruginosa.PLoS pathogens · 2025Article
- Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Divergent genetic landscapes drive lower levels of AmpC induction and stable de-repression inAntimicrobial agents and chemotherapy · 2024Article
- Transcriptional Regulators Controlling Virulence inInternational journal of molecular sciences · 2023Review
- Application of 2D-ITC to the Elucidation of the Enzymatic Mechanism ofBiochemistry · 2023Article
- Bacterial virulence regulation through soluble peptidoglycan fragments sensing and response: knowledge gaps and therapeutic potential.FEMS microbiology reviews · 2023Article
- Hijacking the Peptidoglycan Recycling Pathway of Escherichia coli to Produce Muropeptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Article
- Class C β-Lactamases: Molecular Characteristics.Clinical microbiology reviews · 2022Review
- Induction of AmpC-Mediated β-Lactam Resistance Requires a Single Lytic Transglycosylase in Agrobacterium tumefaciens.Applied and environmental microbiology · 2022Article
- β-lactam Resistance inPathogens (Basel, Switzerland) · 2021Review
- Review
- Mechanisms of Resistance to Ceftolozane/Tazobactam in Pseudomonas aeruginosa: Results of the GERPA Multicenter Study.Antimicrobial agents and chemotherapy · 2021Article
- Fluorescence Assessment of the AmpR-Signaling Network ofACS chemical biology · 2020Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
A complex link exists between cell-wall recycling/repair and the manifestation of resistance to β-lactam antibiotics in many Enterobacteriaceae and Pseudomonas aeruginosa. This process is mediated by specific cell-wall-derived muropeptide products. These muropeptides are internalized into the cytoplasm and bind to the transcriptional regulator AmpR, which controls the cytoplasmic events that lead to expression of β-lactamase, an antibiotic-resistance determinant. The effector-binding domain (EBD) of AmpR was purified to homogeneity. We document that the EBD exists exclusively as a dimer, even at a concentration as low as 1 μM. The EBD binds to the suppressor ligand UDP-N-acetyl-β-d-muramyl-l-Ala-γ-d-Glu-meso-DAP-d-Ala-d-Ala and binds to two activator muropeptides, N-acetyl-β-d-glucosamine-(1→4)-1,6-anhydro-N-acetyl-β-d-muramyl-l-Ala-γ-d-Glu-meso-DAP-d-Ala-d-Ala and 1,6-anhydro-N-acetyl-β-d-muramyl-l-Ala-γ-d-Glu-meso-DAP-d-Ala-d-Ala, as assessed by non-denaturing mass spectrometry. The EBD does not bind to 1,6-anhydro-N-acetyl-β-d-muramyl-l-Ala-γ-d-Glu-meso-DAP. This binding selectivity revises the dogma in the field. The crystal structure of the EBD dimer was solved to 2.2 Å resolution. The EBD crystallizes in a "closed" conformation, in contrast to the "open" structure required to bind the muropeptides. Structural issues of this ligand recognition are addressed by molecular dynamics simulations, which reveal significant differences among the complexes with the effector molecules.
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Registered trials
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.