Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Selective silencing of antibiotic-tethered ribosomes as a resistance mechanism against aminoglycosides.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 9568, Year 2025
Publish date	Oct 29, 2025
Authors	Nilanjan Ghosh Dastidar / Nicola S Freyer / Valentyn Petrychenko / Ana C de A P Schwarzer / Bee-Zen Peng / Ekaterina Samatova / Christina Kothe / Marlen Schmidt / Frank Peske / Antonio Z Politi / Henning Urlaub / Niels Fischer / Marina V Rodnina / Ingo Wohlgemuth /
PubMed Abstract	Antibiotic resistance is a growing threat, underscoring the need to understand the underlying mechanisms. Aminoglycosides kill bacteria by disrupting translation fidelity, leading to the synthesis of ...Antibiotic resistance is a growing threat, underscoring the need to understand the underlying mechanisms. Aminoglycosides kill bacteria by disrupting translation fidelity, leading to the synthesis of aberrant proteins. Surprisingly, mutations in fusA, a gene encoding translation elongation factor G (EF-G), frequently confer resistance, even though EF-G neither participates in mRNA decoding nor blocks aminoglycoside binding. Here, we show that EF-G resistance variants selectively slow ribosome movement along mRNA when aminoglycosides are bound. This delay increases the chance that the drug dissociates before misreading occurs. Over several elongation cycles, this selective silencing of drug-bound ribosomes prevents error cluster formation, preserving proteome and membrane integrity. As a result, fusA mutations confer resistance early in treatment by preventing self-promoted aminoglycoside uptake. Translation on drug-free ribosomes remains sufficiently rapid to sustain near-normal bacterial growth. The mechanism of selective silencing of corrupted targets reveals a previously unrecognized antibiotic resistance strategy with potential therapeutic implications.
External links	Nat Commun / PubMed:41162373 / PubMed Central
Methods	EM (single particle)
Resolution	2.53 - 9.5 Å
Structure data	54253 9rtu EMDB-54253: Structure of 70S ribosome-EF-G(P610L)-GDP-Pi-apramycin complex with tRNAs in hybrid state 1 (H1- EF-G(P610L)-GDP-Pi) PDB-9rtu: Structure of the 70S-EF-G(P610L)-GDP-Pi ribosome complex with tRNAs in hybrid state 1 (H1-EF-G(P610L)-GDP-Pi) Method: EM (single particle) / Resolution: 3.0 Å 54254 9rtv EMDB-54254: Structure of 70S ribosome-EF-G(P610L)-GDP-Pi-apramycin complex with tRNAs in hybrid state 2 (H2- EF-G(P610L)-GDP-Pi) PDB-9rtv: Structure of the 70S-EF-G(P610L)-GDP-Pi ribosome complex with tRNAs in hybrid state 2 (H2-EF-G(P610L)-GDP-Pi) Method: EM (single particle) / Resolution: 3.6 Å EMDB-55123: Structure of 70S ribosome-apramycin complex with tRNAs in classic state (C) Method: EM (single particle) / Resolution: 2.53 Å EMDB-55124: Structure of 70S ribosome-apramycin complex with tRNAs in hybrid state 1 (H1) Method: EM (single particle) / Resolution: 4.33 Å EMDB-55125: Structure of 70S ribosome-apramycin complex with tRNAs in hybrid state 2 (H2) Method: EM (single particle) / Resolution: 9.5 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ZN: Unknown entry ChemComp-NA: Unknown entry ChemComp-AM2: APRAMYCIN / antibioticYM ChemComp-PO4: PHOSPHATE ION ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM
Source	escherichia coli k-12 (bacteria)
Keywords	RIBOSOME / EF-G / robosome / 70S / apramycin / translocation / mutation