6G96

Crystal structure of TacT3 (tRNA acetylating toxin) from Salmonella

Summary for 6G96

• Entry DOI: 10.2210/pdb6g96/pdb
• Related: 5FVJ
• Descriptor: Acetyltransferase, ACETYL COENZYME *A, BICINE, ... (5 entities in total)
• Functional Keywords: acetyltransferase, toxin, transferase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 40148.18

Authors

Grabe, G.J.,Rycroft, J.A.,Gollan, B.,Hall, A.,Cheverton, A.M.,Larrouy-Maumus, G.,Hare, S.A.,Helaine, S. (deposition date: 2018-04-10, release date: 2018-05-16, Last modification date: 2024-01-17)

Primary citation

Rycroft, J.A.,Gollan, B.,Grabe, G.J.,Hall, A.,Cheverton, A.M.,Larrouy-Maumus, G.,Hare, S.A.,Helaine, S.
Activity of acetyltransferase toxins involved in Salmonella persister formation during macrophage infection.
Nat Commun, 9:1993-1993, 2018

PubMed Abstract: Non-typhoidal Salmonella strains are responsible for invasive infections associated with high mortality and recurrence in sub-Saharan Africa, and there is strong evidence for clonal relapse following antibiotic treatment. Persisters are non-growing bacteria that are thought to be responsible for the recalcitrance of many infections to antibiotics. Toxin-antitoxin systems are stress-responsive elements that are important for Salmonella persister formation, specifically during infection. Here, we report the analysis of persister formation of clinical invasive strains of Salmonella Typhimurium and Enteritidis in human primary macrophages. We show that all the invasive clinical isolates of both serovars that we tested produce high levels of persisters following internalization by human macrophages. Our genome comparison reveals that S. Enteritidis and S. Typhimurium strains contain three acetyltransferase toxins that we characterize structurally and functionally. We show that all induce the persister state by inhibiting translation through acetylation of aminoacyl-tRNAs. However, they differ in their potency and target partially different subsets of aminoacyl-tRNAs, potentially accounting for their non-redundant effect.

PubMed: 29777131
DOI: 10.1038/s41467-018-04472-6

Experimental method

X-RAY DIFFRACTION (1.47660774104 Å)