ArticleNature chemical biology2018
Structural basis of protein arginine rhamnosylation by glycosyltransferase EarP.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Vacuolar iron transporters mediate resistance to triadimefon in plant pathogenic fungi.Nature communications · 2026Article
- Mechanism of Bacterial ArginineACS catalysis · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Article
- Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a potential drug targets.BBA advances · 2023Article
- A β-hairpin epitope as novel structural requirement for protein arginine rhamnosylation.Chemical science · 2020Article
- Biochemical characterization of a glycosyltransferase Gtf3 from3 Biotech · 2020Article
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Complex Structure ofJournal of bacteriology · 2019Article
- Switching the Post-translational Modification of Translation Elongation Factor EF-P.Frontiers in microbiology · 2019Article
- Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.Nature communications · 2018Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein glycosylation regulates many cellular processes. Numerous glycosyltransferases with broad substrate specificities have been structurally characterized. A novel inverting glycosyltransferase, EarP, specifically transfers rhamnose from dTDP-β-L-rhamnose to Arg32 of bacterial translation elongation factor P (EF-P) to activate its function. Here we report a crystallographic study of Neisseria meningitidis EarP. The EarP structure contains two tandem Rossmann-fold domains, which classifies EarP in glycosyltransferase superfamily B. In contrast to other structurally characterized protein glycosyltransferases, EarP binds the entire β-sheet structure of EF-P domain I through numerous interactions that specifically recognize its conserved residues. Thus Arg32 is properly located at the active site, and causes structural change in a conserved dTDP-β-L-rhamnose-binding loop of EarP. Rhamnosylation by EarP should occur via an S
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