ArticleScientific reports2019
Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- The Complexity of erm-Mediated Resistance: Structural and Functional Perspectives From β-Hemolytic Streptococci.Molecular microbiology · 2026Review
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Antimicrobial Resistance: Enzymes, Proteins, and Computational Resources.Current pharmaceutical design · 2026Review
- Phylogenetic and Genomic Feature Analysis of CutaneousInfection and drug resistance · 2026Article
- Mechanistic insights into 50Science advances · 2025Article
- Computational investigation of natural compounds as inhibitors against macrolide-resistant protein using virtual screening, molecular docking and MD simulations.Scientific reports · 2025Article
- Article
- Two dynamic N-terminal regions are required for function in ribosomal RNA adenine dimethylase family members.RNA (New York, N.Y.) · 2025Article
- Refactoring the pikromycin synthase for the modular biosynthesis of macrolide antibiotics in E. coli.Research square · 2025Article
- Cyclophostin and Cyclipostins analogues counteract macrolide-induced resistance mediated by erm(41) in Mycobacterium abscessus.Journal of biomedical science · 2024Article
- The resistomes of Mycobacteroides abscessus complex and their possible acquisition from horizontal gene transfer.BMC genomics · 2022Article
- Crystal structure and functional analysis of mycobacterial erythromycin resistance methyltransferase Erm38 reveals its RNA-binding site.The Journal of biological chemistry · 2022Article
- Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA.RNA (New York, N.Y.) · 2022Article
- Molecular docking and pharmacokinetic prediction of phytochemicals fromBiotechnologia · 2022Article
- Exploring Prediction of Antimicrobial Resistance Based on Protein Solvent Accessibility Variation.Frontiers in genetics · 2021Article
- Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition.The Journal of biological chemistry · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Pathogens often receive antibiotic resistance genes through horizontal gene transfer from bacteria that produce natural antibiotics. ErmE is a methyltransferase (MTase) from Saccharopolyspora erythraea that dimethylates A2058 in 23S rRNA using S-adenosyl methionine (SAM) as methyl donor, protecting the ribosomes from macrolide binding. To gain insights into the mechanism of macrolide resistance, the crystal structure of ErmE was determined to 1.75 Å resolution. ErmE consists of an N-terminal Rossmann-like α/ß catalytic domain and a C-terminal helical domain. Comparison with ErmC' that despite only 24% sequence identity has the same function, reveals highly similar catalytic domains. Accordingly, superposition with the catalytic domain of ErmC' in complex with SAM suggests that the cofactor binding site is conserved. The two structures mainly differ in the C-terminal domain, which in ErmE contains a longer loop harboring an additional 3
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