5fvj

Crystal structure of TacT (tRNA acetylating toxin) from Salmonella

spinqualitylabelsall models 5fvj, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fvj is a 2 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The recalcitrance of many bacterial infections to antibiotic treatment is thought to be due to the presence of persisters that are non-growing, antibiotic-insensitive cells. Eventually, persisters resume growth, accounting for relapses of infection. Salmonella is an important pathogen that causes disease through its ability to survive inside macrophages. After macrophage phagocytosis, a significant proportion of the Salmonella population forms non-growing persisters through the action of toxin-antitoxin modules. Here we reveal that one such toxin, TacT, is an acetyltransferase that blocks the primary amine group of amino acids on charged tRNA molecules, thereby inhibiting translation and promoting persister formation. Furthermore, we report the crystal structure of TacT and note unique structural features, including two positively charged surface patches that are essential for toxicity. Finally, we identify a detoxifying mechanism in Salmonella wherein peptidyl-tRNA hydrolase counteracts TacT-dependent growth arrest, explaining how bacterial persisters can resume growth. A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.,Cheverton AM, Gollan B, Przydacz M, Wong CT, Mylona A, Hare SA, Helaine S Mol Cell. 2016 May 31. pii: S1097-2765(16)30139-3. doi:, 10.1016/j.molcel.2016.05.002. PMID:27264868 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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