Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural mechanism of FusB-mediated rescue from fusidic acid inhibition of protein synthesis.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 3693, Year 2025
Publish date	Apr 18, 2025
Authors	Adrián González-López / Xueliang Ge / Daniel S D Larsson / Carina Sihlbom Wallem / Suparna Sanyal / Maria Selmer /
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 ...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.
External links	Nat Commun / PubMed:40251147 / PubMed Central
Methods	EM (single particle)
Resolution	1.87 - 2.79 Å
Structure data	51350 9gha EMDB-51350, PDB-9gha: Fusidic acid-locked Escherichia coli 70S ribosome with Staphylococcus aureus EF-G and a tRNA in pe/E chimeric state (CHI) Method: EM (single particle) / Resolution: 2.24 Å 51351 9ghb EMDB-51351, PDB-9ghb: Fusidic acid-locked Escherichia coli 70S ribosome with Staphylococcus aureus EF-G in post-translocational state (POST) Method: EM (single particle) / Resolution: 2.21 Å 51352 9ghc EMDB-51352, PDB-9ghc: Pre-release fusidic acid-locked Escherichia coli 70S ribosome with Staphylococus aureus EF-G and FusB (FusB-EF-G-70S) Method: EM (single particle) / Resolution: 2.79 Å 51353 9ghd EMDB-51353, PDB-9ghd: Escherichia coli 70S ribosome in complex with Staphylococcus aureus FusB-EF-G (FusB-EF-G-70S) Method: EM (single particle) / Resolution: 2.41 Å 51354 9ghe EMDB-51354, PDB-9ghe: Staphylococcus aureus FusB bound to the small subunit of the Escherichia coli 70S ribosome (FusB-70S:SSU)* Method: EM (single particle) / Resolution: 1.87 Å 51355 9ghf EMDB-51355, PDB-9ghf: Staphylococcus aureus FusB bound to the large subunit of the Escherichia coli 70S ribosome (FusB-70S:LSU) Method: EM (single particle) / Resolution: 2.4 Å 51356 9ghg EMDB-51356, PDB-9ghg: Staphylococcus aureus FusB bound to the small subunit of the S. aureus 70S ribosome (FusB-Sa70S:SSU) Method: EM (single particle) / Resolution: 2.22 Å 51357 9ghh EMDB-51357, PDB-9ghh: Staphylococcus aureus FusB bound to the large subunit of the S. aureus 70S ribosome (FusB-Sa70S:LSU) Method: EM (single particle) / Resolution: 2.7 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-K: Unknown entry ChemComp-MG: Unknown entry ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM ChemComp-FUA: FUSIDIC ACID / antibiotic, AntimicrobialYM ChemComp-HOH: WATER ChemComp-PUT: 1,4-DIAMINOBUTANE
Source	staphylococcus aureus subsp. aureus nctc 8325 (bacteria) escherichia coli k-12 (bacteria) staphylococcus aureus (bacteria)
Keywords	RIBOSOME / fusidic acid / EF-G / antibiotic / FusB