8CGK

Lincomycin and Avilamycin bound to the 50S subunit

8CGK の概要

• エントリーDOI: 10.2210/pdb8cgk/pdb
• 関連するPDBエントリー: 8CA7 8CAI 8CAM 8CAZ 8CEP 8CEU 8CF1 8CF8 8CGD 8CGI 8CGJ 8CGR 8CGU 8CGV
• EMDBエントリー: 16520 16526 16530 16536 16612 16613 16615 16620 16641 16644 16645 16646 16650 16651 16652
• 分子名称: Large ribosomal subunit protein bL33, Large ribosomal subunit protein uL6, Large ribosomal subunit protein bL9, ... (35 entities in total)
• 機能のキーワード: antibiotic, ribosome
• 由来する生物種: Escherichia coli BW25113; 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 1321188.08

構造登録者

Paternoga, H.,Crowe-McAuliffe, C.,Beckert, B.,Wilson, D.N. (登録日: 2023-02-05, 公開日: 2023-07-19, 最終更新日: 2023-11-15)

主引用文献

Paternoga, H.,Crowe-McAuliffe, C.,Bock, L.V.,Koller, T.O.,Morici, M.,Beckert, B.,Myasnikov, A.G.,Grubmuller, H.,Novacek, J.,Wilson, D.N.
Structural conservation of antibiotic interaction with ribosomes.
Nat.Struct.Mol.Biol., 30:1380-1392, 2023

PubMed Abstract: The ribosome is a major target for clinically used antibiotics, but multidrug resistant pathogenic bacteria are making our current arsenal of antimicrobials obsolete. Here we present cryo-electron-microscopy structures of 17 distinct compounds from six different antibiotic classes bound to the bacterial ribosome at resolutions ranging from 1.6 to 2.2 Å. The improved resolution enables a precise description of antibiotic-ribosome interactions, encompassing solvent networks that mediate multiple additional interactions between the drugs and their target. Our results reveal a high structural conservation in the binding mode between antibiotics with the same scaffold, including ordered water molecules. Water molecules are visualized within the antibiotic binding sites that are preordered, become ordered in the presence of the drug and that are physically displaced on drug binding. Insight into RNA-ligand interactions will facilitate development of new antimicrobial agents, as well as other RNA-targeting therapies.

PubMed: 37550453
DOI: 10.1038/s41594-023-01047-y

実験手法

ELECTRON MICROSCOPY (1.64 Å)