EMD-10283
Pseudomonas aeruginosa 30s ribosome from a clinical isolate
EMD-10283
Single-particle3.6 Å
Deposition: 01/09/2019
Map released: 16/10/2019
Last modified: 16/10/2024
Sample Organism:
Pseudomonas aeruginosa
Sample: Pseudomonas aeruginosa 70s ribosome from a clinical isolate
Fitted models: 6spe (Avg. Q-score: 0.46)
Deposition Authors: Halfon Y, Jimenez-Fernande A
Sample: Pseudomonas aeruginosa 70s ribosome from a clinical isolate
Fitted models: 6spe (Avg. Q-score: 0.46)
Deposition Authors: Halfon Y, Jimenez-Fernande A
Structure ofPseudomonas aeruginosaribosomes from an aminoglycoside-resistant clinical isolate.
Halfon Y,
Jimenez-Fernandez A ,
La Rosa R ,
Espinosa Portero R,
Krogh Johansen H ,
Matzov D,
Eyal Z,
Bashan A,
Zimmerman E,
Belousoff M ,
Molin S ,
Yonath A
(2019) PNAS , 116 , 22275 - 22281
(2019) PNAS , 116 , 22275 - 22281
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.
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.