ArticleProceedings of the National Academy of Sciences of the United States of America2015
Cryo-EM structure of the tetracycline resistance protein TetM in complex with a translating ribosome at 3.9-Å resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 64 citations in OpenAlex.
- Multiple Independent Origins of TnAntibiotics (Basel, Switzerland) · 2026Article
- Interplay of the ribosome A and CAR sites.NAR genomics and bioinformatics · 2026Article
- [Molecular mechanisms underlying the development and spread of antibiotic resistance].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2026Review
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- Binding assays enable discovery of Tet(X) inhibitors that combat tetracycline destructase resistance.Chemical science · 2025Article
- The tetracycline resistome is shaped by selection for specific resistance mechanisms by each antibiotic generation.Nature communications · 2025Article
- In vitro Activity of the Novel Tetracyclines Derivative, Zifanocycline AgainstInfection and drug resistance · 2025Article
- The tigecycline resistance mechanisms in Gram-negative bacilli.Frontiers in cellular and infection microbiology · 2024Review
- Ribosome-targeting antibiotics and resistanceRSC medicinal chemistry · 2023Review
- The Myxobacterial Antibiotic Myxovalargin: Biosynthesis, Structural Revision, Total Synthesis, and Molecular Characterization of Ribosomal Inhibition.Journal of the American Chemical Society · 2023Article
- Whole-genome sequencing ofFrontiers in microbiology · 2023Article
- Purine metabolism regulatesFrontiers in microbiology · 2023Article
- Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes.Nucleic acids research · 2022Article
- Antibiotic Resistance Risk with Oral Tetracycline Treatment of Acne Vulgaris.Antibiotics (Basel, Switzerland) · 2022Article
- Prediction of Antimicrobial Resistance in Clinical Enterococcus faecium Isolates Using a Rules-Based Analysis of Whole-Genome Sequences.Antimicrobial agents and chemotherapy · 2022Article
- Comparing the taxonomic and functional profiles of gut microbiota from three pig breeds by metagenomic sequencing.Frontiers in genetics · 2022Article
- Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens.Nature communications · 2021Article
- Ribosome Protection Proteins-"New" Players in the Global Arms Race with Antibiotic-Resistant Pathogens.International journal of molecular sciences · 2021Review
- Phenotypic and genetic barriers to establishment of horizontally transferred genes encoding ribosomal protection proteins.The Journal of antimicrobial chemotherapy · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosome protection proteins (RPPs) confer resistance to tetracycline by binding to the ribosome and chasing the drug from its binding site. Current models for RPP action are derived from 7.2- to 16-Å resolution structures of RPPs bound to vacant or nontranslating ribosomes. Here we present a cryo-electron microscopy reconstruction of the RPP TetM in complex with a translating ribosome at 3.9-Å resolution. The structure reveals the contacts of TetM with the ribosome, including interaction between the conserved and functionally critical C-terminal extension of TetM with a unique splayed conformation of nucleotides A1492 and A1493 at the decoding center of the small subunit. The resolution enables us to unambiguously model the side chains of the amino acid residues comprising loop III in domain IV of TetM, revealing that the tyrosine residues Y506 and Y507 are not responsible for drug-release as suggested previously but rather for intrafactor contacts that appear to stabilize the conformation of loop III. Instead, Pro509 at the tip of loop III is located directly within the tetracycline binding site where it interacts with nucleotide C1054 of the 16S rRNA, such that RPP action uses Pro509, rather than Y506/Y507, to directly dislodge and release tetracycline from the ribosome.
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