7RQA
Crystal structure of the Thermus thermophilus 70S ribosome in complex with protein Y, A-site aminoacyl-tRNA analog ACC-PMN, and P-site MTI-tripeptidyl-tRNA analog ACCA-ITM at 2.40A resolution
This is a non-PDB format compatible entry.
Summary for 7RQA
| Entry DOI | 10.2210/pdb7rqa/pdb |
| Descriptor | 23S Ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (63 entities in total) |
| Functional Keywords | chloramphenicol, linezolid, antibiotic, peptidyl-trna, 70s ribosome, inhibition of translation, uncompetitive inhibition, peptidyl transferase center, context-specificity of drug action, ribosome |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 112 |
| Total formula weight | 4432262.38 |
| Authors | Syroegin, E.A.,Flemmich, L.,Klepacki, D.,Vazquez-Laslop, N.,Micura, R.,Polikanov, Y.S. (deposition date: 2021-08-06, release date: 2022-01-26, Last modification date: 2023-11-15) |
| Primary citation | Syroegin, E.A.,Flemmich, L.,Klepacki, D.,Vazquez-Laslop, N.,Micura, R.,Polikanov, Y.S. Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol. Nat.Struct.Mol.Biol., 29:152-161, 2022 Cited by PubMed Abstract: Ribosome-targeting antibiotics serve as powerful antimicrobials and as tools for studying the ribosome, the catalytic peptidyl transferase center (PTC) of which is targeted by many drugs. The classic PTC-acting antibiotic chloramphenicol (CHL) and the newest clinically significant linezolid (LZD) were considered indiscriminate inhibitors of protein synthesis that cause ribosome stalling at every codon of every gene being translated. However, recent discoveries have shown that CHL and LZD preferentially arrest translation when the ribosome needs to polymerize particular amino acid sequences. The molecular mechanisms that underlie the context-specific action of ribosome inhibitors are unknown. Here we present high-resolution structures of ribosomal complexes, with or without CHL, carrying specific nascent peptides that support or negate the drug action. Our data suggest that the penultimate residue of the nascent peptide directly modulates antibiotic affinity to the ribosome by either establishing specific interactions with the drug or by obstructing its proper placement in the binding site. PubMed: 35165455DOI: 10.1038/s41594-022-00720-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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