9GHD

Escherichia coli 70S ribosome in complex with Staphylococcus aureus FusB-EF-G (FusB-EF-G-70S*)

これはPDB形式変換不可エントリーです。

9GHD の概要

• エントリーDOI: 10.2210/pdb9ghd/pdb
• EMDBエントリー: 51353
• 分子名称: Large ribosomal subunit protein bL33, 30S ribosomal protein S4, 30S ribosomal protein S5, ... (59 entities in total)
• 機能のキーワード: ribosome, fusidic acid, ef-g, antibiotic
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 56
• 化学式量合計: 2298973.53

構造登録者

Gonzalez-Lopez, A.,Selmer, M. (登録日: 2024-08-15, 公開日: 2025-03-26, 最終更新日: 2025-04-30)

主引用文献

Gonzalez-Lopez, A.,Ge, X.,Larsson, D.S.D.,Sihlbom Wallem, C.,Sanyal, S.,Selmer, M.
Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis.
Nat Commun, 16:3693-3693, 2025

PubMed Abstract: The antibiotic resistance protein FusB rescues protein synthesis from inhibition by fusidic acid (FA), which locks elongation factor G (EF-G) to the ribosome after GTP hydrolysis. Here, we present time-resolved single-particle cryo-EM structures explaining the mechanism of FusB-mediated rescue. FusB binds to the FA-trapped EF-G on the ribosome, causing large-scale conformational changes of EF-G that break interactions with the ribosome, tRNA, and mRNA. This leads to dissociation of EF-G from the ribosome, followed by FA release. We also observe two independent binding sites of FusB on the classical-state ribosome, overlapping with the binding site of EF-G to each of the ribosomal subunits, yet not inhibiting tRNA delivery. The affinity of FusB to the ribosome and the concentration of FusB in S. aureus during FusB-mediated resistance support that direct binding of FusB to ribosomes could occur in the cell. Our results reveal an intricate resistance mechanism involving specific interactions of FusB with both EF-G and the ribosome, and a non-canonical release pathway of EF-G.

PubMed: 40251147
DOI: 10.1038/s41467-025-58902-3

実験手法

ELECTRON MICROSCOPY (2.41 Å)