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Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis
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Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis
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Journal Article
Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis
2025
Overview
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.
Fusidic acid inhibits translation by locking EF-G to the bacterial ribosome. Here, the authors use cryo-EM to visualize the transient state where resistance protein FusB mediates rescue by inducing large-scale conformational changes of EF-G.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 101/58
/ 82/80
/ 82/83
/ Anti-Bacterial Agents - pharmacology
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biologi med inriktning mot strukturbiologi
/ Biology with specialization in Structural Biology
/ Guanosine Triphosphate - metabolism
/ Humanities and Social Sciences
/ Locks
/ mRNA
/ Peptide Elongation Factor G - chemistry
/ Peptide Elongation Factor G - metabolism
/ Protein Biosynthesis - drug effects
/ Proteins
/ RNA
/ Science
/ Staphylococcus aureus - drug effects
/ Staphylococcus aureus - genetics
/ Staphylococcus aureus - metabolism
/ tRNA
