4V7T

Crystal structure of the E. coli ribosome bound to chloramphenicol.

これはPDB形式変換不可エントリーです。

4V7T の概要

• エントリーDOI: 10.2210/pdb4v7t/pdb
• 関連するPDBエントリー: 3OAQ 3OAR 3OAS 3OAT 3OFB 3OFC 3OFD 3OFO 3OFP 3OFQ 3OFR 3OFX 3OFY 3OFZ 3OG0
• 分子名称: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (63 entities in total)
• 機能のキーワード: protein biosynthesis, ribosomes, rna, trna, transfer, erythromycin, ketolide, macrolide, antibiotic, exit, peptidyl, 30s, 70s, 16s, ribosomal subunit, small, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 104
• 化学式量合計: 4235068.35

構造登録者

Dunkle, J.A.,Xiong, L.,Mankin, A.S.,Cate, J.H.D. (登録日: 2010-08-14, 公開日: 2014-07-09, 最終更新日: 2024-11-27)

主引用文献

Dunkle, J.A.,Xiong, L.,Mankin, A.S.,Cate, J.H.
Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action.
Proc.Natl.Acad.Sci.USA, 107:17152-17157, 2010

PubMed Abstract: Differences between the structures of bacterial, archaeal, and eukaryotic ribosomes account for the selective action of antibiotics. Even minor variations in the structure of ribosomes of different bacterial species may lead to idiosyncratic, species-specific interactions of the drugs with their targets. Although crystallographic structures of antibiotics bound to the peptidyl transferase center or the exit tunnel of archaeal (Haloarcula marismortui) and bacterial (Deinococcus radiodurans) large ribosomal subunits have been reported, it remains unclear whether the interactions of antibiotics with these ribosomes accurately reflect those with the ribosomes of pathogenic bacteria. Here we report X-ray crystal structures of the Escherichia coli ribosome in complexes with clinically important antibiotics of four major classes, including the macrolide erythromycin, the ketolide telithromycin, the lincosamide clindamycin, and a phenicol, chloramphenicol, at resolutions of ∼3.3 Å-3.4 Å. Binding modes of three of these antibiotics show important variations compared to the previously determined structures. Biochemical and structural evidence also indicates that interactions of telithromycin with the E. coli ribosome more closely resembles drug binding to ribosomes of bacterial pathogens. The present data further argue that the identity of nucleotides 752, 2609, and 2055 of 23S ribosomal RNA explain in part the spectrum and selectivity of antibiotic action.

PubMed: 20876128
DOI: 10.1073/pnas.1007988107

実験手法

X-RAY DIFFRACTION (3.1942 Å)