Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of ribosomes from an aminoglycoside-resistant clinical isolate.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 44, Page 22275-22281, Year 2019
Publish date	Oct 29, 2019
Authors	Yehuda Halfon / Alicia Jimenez-Fernandez / Ruggero La Rosa / Rocio Espinosa Portero / Helle Krogh Johansen / Donna Matzov / Zohar Eyal / Anat Bashan / Ella Zimmerman / Matthew Belousoff / Søren Molin / Ada Yonath /
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 ...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.
External links	Proc Natl Acad Sci U S A / PubMed:31611393 / PubMed Central
Methods	EM (single particle)
Resolution	2.82 - 3.6 Å
Structure data	10280 6spb EMDB-10280, PDB-6spb: Pseudomonas aeruginosa 50s ribosome from a clinical isolate with a mutation in uL6 Method: EM (single particle) / Resolution: 2.82 Å 10281 6spc EMDB-10281, PDB-6spc: Pseudomonas aeruginosa 30s ribosome from an aminoglycoside resistant clinical isolate Method: EM (single particle) / Resolution: 2.95 Å 10282 6spd EMDB-10282, PDB-6spd: Pseudomonas aeruginosa 50s ribosome from a clinical isolate Method: EM (single particle) / Resolution: 3.28 Å 10283 6spe EMDB-10283, PDB-6spe: Pseudomonas aeruginosa 30s ribosome from a clinical isolate Method: EM (single particle) / Resolution: 3.6 Å 10284 6spf EMDB-10284, PDB-6spf: Pseudomonas aeruginosa 70s ribosome from an aminoglycoside resistant clinical isolate Method: EM (single particle) / Resolution: 2.89 Å 10285 6spg EMDB-10285, PDB-6spg: Pseudomonas aeruginosa 70s ribosome from a clinical isolate Method: EM (single particle) / Resolution: 3.34 Å
Chemicals	ChemComp-MG: Unknown entry
Source	Pseudomonas aeruginos (bacteria) pseudomonas aeruginosa (bacteria)
Keywords	RIBOSOME / Pseudomonas aeruginosa / mutation