3DLL

The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning

3DLL の概要

• エントリーDOI: 10.2210/pdb3dll/pdb
• 分子名称: rRNA-23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (33 entities in total)
• 機能のキーワード: ribosome, antibiotic, oxazolidinone, linezolid, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, methylation, metal-binding, zinc-finger
• 由来する生物種: Deinococcus radiodurans; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1365757.44

構造登録者

Wilson, D.N.,Schluenzen, F.,Harms, J.M.,Starosta, A.L.,Connell, S.R.,Fucini, P. (登録日: 2008-06-27, 公開日: 2008-09-16, 最終更新日: 2024-10-30)

主引用文献

Wilson, D.N.,Schluenzen, F.,Harms, J.M.,Starosta, A.L.,Connell, S.R.,Fucini, P.
The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning
Proc.Natl.Acad.Sci.Usa, 105:13339-13344, 2008

PubMed Abstract: The oxazolidinones represent the first new class of antibiotics to enter into clinical usage within the past 30 years, but their binding site and mechanism of action has not been fully characterized. We have determined the crystal structure of the oxazolidinone linezolid bound to the Deinococcus radiodurans 50S ribosomal subunit. Linezolid binds in the A site pocket at the peptidyltransferase center of the ribosome overlapping the aminoacyl moiety of an A-site bound tRNA as well as many clinically important antibiotics. Binding of linezolid stabilizes a distinct conformation of the universally conserved 23S rRNA nucleotide U2585 that would be nonproductive for peptide bond formation. In conjunction with available biochemical data, we present a model whereby oxazolidinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome.

PubMed: 18757750
DOI: 10.1073/pnas.0804276105

実験手法

X-RAY DIFFRACTION (3.5 Å)