2YB5

Structure of the fusidic acid resistance protein FusC

Summary for 2YB5

• Entry DOI: 10.2210/pdb2yb5/pdb
• Descriptor: PUTATIVE FUSIDIC ACID RESISTANCE PROTEIN, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: translation, antibiotic resistance, zinc finger
• Biological source: STAPHYLOCOCCUS AUREUS
• Total number of polymer chains: 2
• Total formula weight: 51481.73

Authors

Cox, G.,Edwards, T.A. (deposition date: 2011-03-01, release date: 2012-01-25, Last modification date: 2024-05-08)

Primary citation

Cox, G.,Thompson, G.S.,Jenkins, H.T.,Homans, S.W.,Edwards, T.A.,Oneill, A.J.
Ribosome Clearance by Fusb-Type Proteins Mediates Resistance to the Antibiotic Fusidic Acid
Proc.Natl.Acad.Sci.USA, 109:2102-, 2012

PubMed Abstract: 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.

PubMed: 22308410
DOI: 10.1073/PNAS.1117275109

Experimental method

X-RAY DIFFRACTION (2.1 Å)