9GHC
Pre-release fusidic acid-locked Escherichia coli 70S ribosome with Staphylococus aureus EF-G and FusB (FusB-EF-G-70S)
This is a non-PDB format compatible entry.
Summary for 9GHC
| Entry DOI | 10.2210/pdb9ghc/pdb |
| EMDB information | 51352 |
| Descriptor | 50S ribosomal protein L33, 30S ribosomal protein S4, 30S ribosomal protein S5, ... (61 entities in total) |
| Functional Keywords | ribosome, fusidic acid, ef-g, antibiotic |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 56 |
| Total formula weight | 2299832.94 |
| Authors | Gonzalez-Lopez, A.,Selmer, M. (deposition date: 2024-08-15, release date: 2025-03-26, Last modification date: 2025-04-30) |
| Primary citation | 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 Cited by 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: 40251147DOI: 10.1038/s41467-025-58902-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.79 Å) |
Structure validation
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