ArticleScientific reports2018
First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD.
Article in Scientific reports, 2018. 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, 23 citations in OpenAlex.
- Compositional analysis of bacterial peptidoglycan: insights from peptidoglycomics into structure and function.Journal of bacteriology · 2025Review
- Proteomic and metabolomic responses of priority bacterial pathogens to subinhibitory concentration of antibiotics.npj antimicrobials and resistance · 2025Article
- Performance prediction of polypeptide derivatives as efficient potential microbial inhibitors: a computational approach.International journal of biochemistry and molecular biology · 2024Article
- Metaproteomic Analysis of Gut Resistome in the Cecal Microbiota of Fattening Pigs Raised without Antibiotics.Microbiology spectrum · 2023Article
- CRISPRi-mediated characterization of novel anti-tuberculosis targets: Mycobacterial peptidoglycan modifications promote beta-lactam resistance and intracellular survival.Frontiers in cellular and infection microbiology · 2023Article
- CroR Regulates Expression ofmBio · 2022Article
- Role of MurT C-Terminal Domain in the Amidation of Staphylococcus aureus Peptidoglycan.Antimicrobial agents and chemotherapy · 2019Article
- Cell wall peptidoglycan in Mycobacterium tuberculosis: An Achilles' heel for the TB-causing pathogen.FEMS microbiology reviews · 2019Review
- Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.Scientific reports · 2018Article
- Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.Nature communications · 2018Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-positive bacteria homeostasis and antibiotic resistance mechanisms are dependent on the intricate architecture of the cell wall, where amidated peptidoglycan plays an important role. The amidation reaction is carried out by the bi-enzymatic complex MurT-GatD, for which biochemical and structural information is very scarce. In this work, we report the first crystal structure of the glutamine amidotransferase member of this complex, GatD from Staphylococcus aureus, at 1.85 Å resolution. A glutamine molecule is found close to the active site funnel, hydrogen-bonded to the conserved R128. In vitro functional studies using
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