ArticleJournal of the American Chemical Society2014
Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- Chaotropic ions reshape the cell wall of the obligate halophile aspergillus atacamensis: Insights from solid-state NMR.Carbohydrate polymers · 2026Article
- Chaotropic Ions Reshape the Cell Wall of the Obligate HalophilebioRxiv : the preprint server for biology · 2026Article
- Lipopolysaccharide nanoparticles: A biomimetic platform to study bacterial surface.Biophysical journal · 2025Article
- Biochemical and crystallographic studies of L,D-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate.Communications biology · 2024Article
- Solid-state NMR structure determination of a membrane protein inScience advances · 2023Article
- Staphylococcus aureus sacculus mediates activities of M23 hydrolases.Nature communications · 2023Article
- Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases.Acta crystallographica. Section D, Structural biology · 2023Article
- Article
- Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants.Chemical reviews · 2022Review
- From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR.Chemical reviews · 2022Review
- Article
- Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.Nature protocols · 2021Article
- Development of in vitro-grown spheroids as a 3D tumor model system for solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
- Fast MASJournal of biomolecular NMR · 2019Article
- Review
- Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli.Nature communications · 2019Article
- Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency.Journal of structural biology · 2019Article
- Rapid access to RNA resonances by proton-detected solid-state NMR at >100 kHz MAS.Chemical communications (Cambridge, England) · 2018Article
- Recognition of Peptidoglycan Fragments by the Transpeptidase PBP4 FromFrontiers in microbiology · 2018Article
- Characterization of the Conjugation Pattern in Large Polysaccharide-Protein Conjugates by NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2017Article
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Authors and funding
8 authors at 6 institutions in 1 country.
Funding
Abstract
The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a highly cross-linked biopolymer. The transpeptidases that perform this cross-linking are important targets for antibiotics. Despite this biomedical importance, to date no structure of a protein in complex with an intact bacterial peptidoglycan has been resolved, primarily due to the large size and flexibility of peptidoglycan sacculi. Here we use solid-state NMR spectroscopy to derive for the first time an atomic model of an l,d-transpeptidase from Bacillus subtilis bound to its natural substrate, the intact B. subtilis peptidoglycan. Importantly, the model obtained from protein chemical shift perturbation data shows that both domains-the catalytic domain as well as the proposed peptidoglycan recognition domain-are important for the interaction and reveals a novel binding motif that involves residues outside of the classical enzymatic pocket. Experiments on mutants and truncated protein constructs independently confirm the binding site and the implication of both domains. Through measurements of dipolar-coupling derived order parameters of bond motion we show that protein binding reduces the flexibility of peptidoglycan. This first report of an atomic model of a protein-peptidoglycan complex paves the way for the design of new antibiotic drugs targeting l,d-transpeptidases. The strategy developed here can be extended to the study of a large variety of enzymes involved in peptidoglycan morphogenesis.
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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.