6SPD

Pseudomonas aeruginosa 50s ribosome from a clinical isolate

Summary for 6SPD

• Entry DOI: 10.2210/pdb6spd/pdb
• EMDB information: 10282
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (32 entities in total)
• Functional Keywords: ribosome, pseudomonas aeruginosa
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 32
• Total formula weight: 1354513.84

Authors

Halfon, Y.,Jimenez-Fernande, A.,La Ros, R.,Espinos, R.,Krogh Johansen, H.,Matzov, D.,Eyal, Z.,Bashan, A.,Zimmerman, E.,Belousoff, M.,Molin, S.,Yonath, A. (deposition date: 2019-09-01, release date: 2019-10-16, Last modification date: 2019-11-06)

Primary citation

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.
Structure ofPseudomonas aeruginosaribosomes from an aminoglycoside-resistant clinical isolate.
Proc.Natl.Acad.Sci.USA, 116:22275-22281, 2019

PubMed 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 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.

PubMed: 31611393
DOI: 10.1073/pnas.1909831116

Experimental method

ELECTRON MICROSCOPY (3.28 Å)