8S2N

Xenorhabdus bovienii Rhs toxin TreTu complex with TrxA and TriTu immunity protein

8S2N の概要

• エントリーDOI: 10.2210/pdb8s2n/pdb
• 分子名称: Immunity Protein TriX, Complete genome segment 11/17, Thioredoxin 1, ... (6 entities in total)
• 機能のキーワード: adp-ribosyltransferase, thioredoxin, toxin
• 由来する生物種: Xenorhabdus bovienii SS-2004; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44272.97

構造登録者

Jurenas, D.,Terradot, L. (登録日: 2024-02-18, 公開日: 2024-12-04, 最終更新日: 2024-12-11)

主引用文献

Dumont, B.,Terradot, L.,Cascales, E.,Van Melderen, L.,Jurenas, D.
Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.
Nat Commun, 15:10388-10388, 2024

PubMed Abstract: Formation and breakage of disulfide bridges strongly impacts folding and activity of proteins. Thioredoxin 1 (TrxA) is a small, conserved enzyme that reduces disulfide bonds in the bacterial cytosol. In this study, we provide an example of the emergence of a chaperone role for TrxA, which is independent of redox catalysis. We show that the activity of the secreted bacterial ADP-ribosyltransferase (ART) toxin TreX, which does not contain any cysteines, is dependent on TrxA. TreX binds to the reduced form of TrxA via its carboxy-terminal extension to form a soluble and active complex. Structural studies revealed that TreX-like toxins are homologous to Scabin-like ART toxins which possess cysteine residues and form disulfide bridges at the position that superimposes the TrxA binding site in TreX. Our study therefore suggests that thioredoxin 1 evolved alternative functions by maintaining the interaction with cysteine-free substrates.

PubMed: 39613764
DOI: 10.1038/s41467-024-54892-w

実験手法

X-RAY DIFFRACTION (2.11 Å)