2yb5 | pdb_00002yb5

Structure of the fusidic acid resistance protein FusC

spinqualitylabelsall models 2yb5, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yb5 is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: EDO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1XHT1_STAAU Publication Abstract from PubMed 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 ribosomeEF-GGDP 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. Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid.,Cox G, Thompson GS, Jenkins HT, Peske F, Savelsbergh A, Rodnina MV, Wintermeyer W, Homans SW, Edwards TA, O'Neill AJ Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):2102-7. Epub 2012 Jan 20. PMID:22308410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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