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From the same journal

Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid

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Published copy (DOI)


  • Georgina Cox
  • Gary S Thompson
  • Huw T Jenkins
  • Frank Peske
  • Andreas Savelsbergh
  • Marina V Rodnina
  • Wolfgang Wintermeyer
  • Steve W Homans
  • Thomas A Edwards
  • Alexander J O'Neill


Publication details

JournalProceedings of the National Academy of Sciences of the United States of America
DatePublished - 7 Feb 2012
Issue number6
Pages (from-to)2102-2107
Original languageEnglish


Resistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-mediated inhibition by an unknown mechanism. Here we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains a four-cysteine zinc finger with a unique structural fold. This domain mediates a high-affinity interaction with the C-terminal domains of EF-G. By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosome⋅EF-G⋅GDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation. Ribosome clearance by these proteins represents a highly unusual antibiotic resistance mechanism, which appears to be fine-tuned by the relative abundance of FusB-type protein, ribosomes, and EF-G.

    Research areas

  • Anti-Bacterial Agents, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Drug Resistance, Bacterial, Fusidic Acid, Humans, Models, Biological, Models, Molecular, Peptide Elongation Factor G, Protein Binding, Protein Interaction Maps, Ribosomes

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