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- W2980778913 abstract "Resistance to antibiotics has become a major threat to modern medicine. The ribosome plays a fundamental role in cell vitality by the translation of the genetic code into proteins; hence, it is a major target for clinically useful antibiotics. We report here the cryo-electron microscopy structures of the ribosome of a pathogenic aminoglycoside (AG)-resistant Pseudomonas aeruginosa strain, as well as of a nonresistance strain isolated from a cystic fibrosis patient. The structural studies disclosed defective ribosome complex formation due to a conformational change of rRNA helix H69, an essential intersubunit bridge, and a secondary binding site of the AGs. In addition, a stable conformation of nucleotides A1486 and A1487, pointing into helix h44, is created compared to a non-AG-bound ribosome. We suggest that altering the conformations of ribosomal protein uL6 and rRNA helix H69, which interact with initiation-factor IF2, interferes with proper protein synthesis initiation." @default.
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- W2980778913 date "2019-10-14" @default.
- W2980778913 modified "2023-10-15" @default.
- W2980778913 title "Structure of <i>Pseudomonas aeruginosa</i> ribosomes from an aminoglycoside-resistant clinical isolate" @default.
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- W2980778913 doi "https://doi.org/10.1073/pnas.1909831116" @default.
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