SNAP annotations: PDB entry 6spg

PDB-id

6spg; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (3.34 Å)

Summary

Pseudomonas aeruginosa 70s ribosome from a clinical isolate

Reference

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): "Structure ofPseudomonas aeruginosaribosomes from an aminoglycoside-resistant clinical isolate." Proc.Natl.Acad.Sci.USA, 116, 22275-22281. doi: 10.1073/pnas.1909831116.

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 <i>Pseudomonas aeruginosa</i> 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.