ArticleThe Journal of biological chemistry2015
Crystal Structure of the N-Acetylmuramic Acid α-1-Phosphate (MurNAc-α1-P) Uridylyltransferase MurU, a Minimal Sugar Nucleotidyltransferase and Potential Drug Target Enzyme in Gram-negative Pathogens.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Metabolic flexibility and an unusual route for peptidoglycan muramic acid recycling in mycobacteria.The Journal of biological chemistry · 2026Article
- Biosynthesis of glycosylated 5-hydroxycytosine in the DNA of diverse viruses.Nucleic acids research · 2026Article
- Enzymatic activities of proteins encoded by PmurB, PmurC, and PmurE involved in methanogen pseudomurein biosynthesis.Frontiers in microbiology · 2026Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Differences in Fosfomycin Resistance Mechanisms between Pseudomonas aeruginosa andAntimicrobial agents and chemotherapy · 2022Review
- Mechanism of Nucleotidyltransfer Reaction and Role of MgBiophysical journal · 2020Article
- GTP Preference of d-Glycero-α-d-International journal of molecular sciences · 2019Article
- Synthesis of Functionalized N-Acetyl Muramic Acids To Probe Bacterial Cell Wall Recycling and Biosynthesis.Journal of the American Chemical Society · 2018Article
- Article
- Peptidoglycan Recycling in Gram-Positive Bacteria Is Crucial for Survival in Stationary Phase.mBio · 2016Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-acetylmuramic acid α-1-phosphate (MurNAc-α1-P) uridylyltransferase MurU catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall. MurU is part of a recently identified cell wall recycling pathway in Gram-negative bacteria that bypasses the general de novo biosynthesis of UDP-MurNAc and contributes to high intrinsic resistance to the antibiotic fosfomycin, which targets UDP-MurNAc de novo biosynthesis. To provide insights into substrate binding and specificity, we solved crystal structures of MurU of Pseudomonas putida in native and ligand-bound states at high resolution. With the help of these structures, critical enzyme-substrate interactions were identified that enable tight binding of MurNAc-α1-P to the active site of MurU. The MurU structures define a "minimal domain" required for general nucleotidyltransferase activity. They furthermore provide a structural basis for the chemical design of inhibitors of MurU that could serve as novel drugs in combination therapy against multidrug-resistant Gram-negative pathogens.
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