7ZG5

The crystal structure of Salmonella TacAT3-DNA complex

7ZG5 の概要

• エントリーDOI: 10.2210/pdb7zg5/pdb
• 分子名称: Acetyltransferase, DUF1778 domain-containing protein, tacAT3 DNA operator, ... (9 entities in total)
• 機能のキーワード: toxin-antitoxin system, salmonella, acetyltransferase, conditional cooperativity, toxin
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 68539.94

構造登録者

Grabe, G.J.,Morgan, R.M.L.,Helaine, S. (登録日: 2022-04-01, 公開日: 2023-10-11, 最終更新日: 2026-03-04)

主引用文献

Grabe, G.J.,Giorgio, R.T.,Wieczor, M.,Gollan, B.,Sargen, M.,Orozco, M.,Hare, S.A.,Helaine, S.
Molecular stripping underpins derepression of a toxin-antitoxin system.
Nat.Struct.Mol.Biol., 2024

PubMed Abstract: Transcription factors control gene expression; among these, transcriptional repressors must liberate the promoter for derepression to occur. Toxin-antitoxin (TA) modules are bacterial elements that autoregulate their transcription by binding the promoter in a T:A ratio-dependent manner, known as conditional cooperativity. The molecular basis of how excess toxin triggers derepression has remained elusive, largely because monitoring the rearrangement of promoter-repressor complexes, which underpin derepression, is challenging. Here, we dissect the autoregulation of the Salmonella enterica tacAT3 module. Using a combination of assays targeting DNA binding and promoter activity, as well as structural characterization, we determine the essential TA and DNA elements required to control transcription, and we reconstitute a repression-to-derepression path. We demonstrate that excess toxin triggers molecular stripping of the repressor complex off the DNA through multiple allosteric changes causing DNA distortion and ultimately leading to derepression. Thus, our work provides important insight into the mechanisms underlying conditional cooperativity.

PubMed: 38538913
DOI: 10.1038/s41594-024-01253-2

実験手法

X-RAY DIFFRACTION (2 Å)