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6SPC

Pseudomonas aeruginosa 30s ribosome from an aminoglycoside resistant clinical isolate

6SPC の概要
エントリーDOI10.2210/pdb6spc/pdb
EMDBエントリー10281
分子名称16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (21 entities in total)
機能のキーワードribosome, pseudomonas aeruginosa
由来する生物種Pseudomonas aeruginosa
詳細
タンパク質・核酸の鎖数21
化学式量合計752360.85
構造登録者
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.95 Å)
構造検証レポート
Validation report summary of 6spc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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