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TitleStructures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane.
Journal, issue, pagesSci Rep, Vol. 14, Issue 1, Page 14253, Year 2024
Publish dateJun 20, 2024
AuthorsAdrián González-López / Daniel S D Larsson / Ravi Kiran Koripella / Brett N Cain / Martin Garcia Chavez / Paul J Hergenrother / Suparna Sanyal / Maria Selmer /
PubMed AbstractThe antibiotic fusidic acid (FA) is used to treat Staphylococcus aureus infections. It inhibits protein synthesis by binding to elongation factor G (EF-G) and preventing its release from the ribosome ...The antibiotic fusidic acid (FA) is used to treat Staphylococcus aureus infections. It inhibits protein synthesis by binding to elongation factor G (EF-G) and preventing its release from the ribosome after translocation. While FA, due to permeability issues, is only effective against gram-positive bacteria, the available structures of FA-inhibited complexes are from gram-negative model organisms. To fill this knowledge gap, we solved cryo-EM structures of the S. aureus ribosome in complex with mRNA, tRNA, EF-G and FA to 2.5 Å resolution and the corresponding complex structures with the recently developed FA derivative FA-cyclopentane (FA-CP) to 2.0 Å resolution. With both FA variants, the majority of the ribosomal particles are observed in chimeric state and only a minor population in post-translocational state. As expected, FA binds in a pocket between domains I, II and III of EF-G and the sarcin-ricin loop of 23S rRNA. FA-CP binds in an identical position, but its cyclopentane moiety provides additional contacts to EF-G and 23S rRNA, suggesting that its improved resistance profile towards mutations in EF-G is due to higher-affinity binding. These high-resolution structures reveal new details about the S. aureus ribosome, including confirmation of many rRNA modifications, and provide an optimal starting point for future structure-based drug discovery on an important clinical drug target.
External linksSci Rep / PubMed:38902339 / PubMed Central
MethodsEM (single particle)
Resolution2.02 - 2.49 Å
Structure data

17363

8p2f

EMDB-17363, PDB-8p2f:
Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid cyclopentane in post-translocational state
Method: EM (single particle) / Resolution: 2.44 Å

17364

8p2g

EMDB-17364: Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid cyclopentane with a tRNA in pe/E chimeric hybrid state
PDB-8p2g: Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid cyclopentane with a tRNA in pe/E chimeric state
Method: EM (single particle) / Resolution: 2.02 Å

17365

8p2h

EMDB-17365, PDB-8p2h:
Staphylococcus aureus 70S ribosome with elongation factor G locked with fusidic acid with a tRNA in pe/E chimeric state
Method: EM (single particle) / Resolution: 2.49 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-SPD:
SPERMIDINE

ChemComp-PUT:
1,4-DIAMINOBUTANE

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM


ChemComp, No image

ChemComp-WUX:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FUA:
FUSIDIC ACID / antibiotic, Antimicrobial*YM

Source
  • staphylococcus aureus subsp. aureus nctc 8325 (bacteria)
  • escherichia coli (E. coli)
KeywordsRIBOSOME / fusidic acid / EF-G / antibiotic

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