6GTQ

Structure of the AtaT Y144F mutant toxin bound to the C-terminus of the antitoxin AtaR

6GTQ の概要

• エントリーDOI: 10.2210/pdb6gtq/pdb
• 分子名称: N-acetyltransferase, DUF1778 domain-containing protein, CHLORIDE ION, ... (9 entities in total)
• 機能のキーワード: ta toxin, antitoxin, n-acetyl transferase, ribbon-helix-helix, rhh, bacterial repressor, transcription, toxin-antitoxin complex
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51455.26

構造登録者

Garcia-Pino, A.,Jurenas, D. (登録日: 2018-06-18, 公開日: 2019-03-06, 最終更新日: 2024-01-17)

主引用文献

Jurenas, D.,Van Melderen, L.,Garcia-Pino, A.
Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system.
Nat. Chem. Biol., 15:285-294, 2019

PubMed Abstract: GCN5-related N-acetyl-transferase (GNAT)-like enzymes from toxin-antitoxin modules are strong inhibitors of protein synthesis. Here, we present the bases of the regulatory mechanisms of ataRT, a model GNAT-toxin-antitoxin module, from toxin synthesis to its action as a transcriptional de-repressor. We show the antitoxin (AtaR) traps the toxin (AtaT) in a pre-catalytic monomeric state and precludes the effective binding of ac-CoA and its target Met-transfer RNA. In the repressor complex, AtaR intrinsically disordered region interacts with AtaT at two different sites, folding into different structures, that are involved in two separate functional roles, toxin neutralization and placing the DNA-binding domains of AtaR in a binding-compatible orientation. Our data suggests AtaR neutralizes AtaT as a monomer, right after its synthesis and only the toxin-antitoxin complex formed in this way is an active repressor. Once activated by dimerization, later neutralization of the toxin results in a toxin-antitoxin complex that is not able to repress transcription.

PubMed: 30718814
DOI: 10.1038/s41589-018-0216-z

実験手法

X-RAY DIFFRACTION (2.49 Å)