5FVJ

Crystal structure of TacT (tRNA acetylating toxin) from Salmonella

5FVJ の概要

• エントリーDOI: 10.2210/pdb5fvj/pdb
• 分子名称: PUTATIVE ACETYLTRANSFERASE, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: transferase, acetyltransferase
• 由来する生物種: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37848.83

構造登録者

Przydacz, M.,Wong, C.T.,Cheverton, A.M.,Gollan, B.,Mylona, A.,Helaine, S.,Hare, S.A. (登録日: 2016-02-08, 公開日: 2016-06-01, 最終更新日: 2024-05-08)

主引用文献

Cheverton, A.M.,Gollan, B.,Przydacz, M.,Wong, C.T.,Mylona, A.,Hare, S.A.,Helaine, S.
A Salmonella Toxin Promotes Persister Formation Through Acetylation of tRNA.
Mol.Cell, 63:86-, 2016

PubMed Abstract: 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.

PubMed: 27264868
DOI: 10.1016/J.MOLCEL.2016.05.002

実験手法

X-RAY DIFFRACTION (1.7 Å)