7AK9

Structure of Salmonella TacT3 toxin bound to TacA3 antitoxin C-terminal peptide

7AK9 の概要

• エントリーDOI: 10.2210/pdb7ak9/pdb
• 分子名称: Acetyltransferase, ABC transporter, DEPHOSPHO COENZYME A, ... (4 entities in total)
• 機能のキーワード: acetyltransferase, toxin, antitoxin, gnat
• 由来する生物種: Salmonella typhimurium; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47746.45

構造登録者

Grabe, G.J.,Morgan, R.M.L.,Hare, S.A.,Helaine, S. (登録日: 2020-09-30, 公開日: 2021-08-18, 最終更新日: 2024-01-31)

主引用文献

Grabe, G.J.,Giorgio, R.T.,Hall, A.M.J.,Morgan, R.M.L.,Dubois, L.,Sisley, T.A.,Rycroft, J.A.,Hare, S.A.,Helaine, S.
Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.
Nat.Chem.Biol., 17:1296-1304, 2021

PubMed Abstract: Toxin-antitoxin (TA) systems are a large family of genes implicated in the regulation of bacterial growth and its arrest in response to attacks. These systems encode nonsecreted toxins and antitoxins that specifically pair, even when present in several paralogous copies per genome. Salmonella enterica serovar Typhimurium contains three paralogous TacAT systems that block bacterial translation. We determined the crystal structures of the three TacAT complexes to understand the structural basis of specific TA neutralization and the evolution of such specific pairing. In the present study, we show that alteration of a discrete structural add-on element on the toxin drives specific recognition by their cognate antitoxin underpinning insulation of the three pairs. Similar to other TA families, the region supporting TA-specific pairing is key to neutralization. Our work reveals that additional TA interfaces beside the main neutralization interface increase the safe space for evolution of pairing specificity.

PubMed: 34556858
DOI: 10.1038/s41589-021-00862-y

実験手法

X-RAY DIFFRACTION (2.55 Å)