8UXT

Acinetobacter baumannii Tse15 Rhs effector, toxin cleavage mutant (D1369N, D1391N)

8UXT の概要

• エントリーDOI: 10.2210/pdb8uxt/pdb
• EMDBエントリー: 42775
• 分子名称: Tse15 (1 entity in total)
• 機能のキーワード: rhs-effector, rhs cargo effector, type 6 secretion system effector, acinetobacter baumannii toxin, yd-repeat protein, t6ss., toxin
• 由来する生物種: Acinetobacter baumannii AB307-0294
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 181545.06

構造登録者

Hayes, B.K.,Venugopal, H.,McGowan, S. (登録日: 2023-11-10, 公開日: 2024-10-09, 最終更新日: 2025-05-14)

主引用文献

Hayes, B.K.,Harper, M.,Venugopal, H.,Lewis, J.M.,Wright, A.,Lee, H.C.,Steele, J.R.,Steer, D.L.,Schittenhelm, R.B.,Boyce, J.D.,McGowan, S.
Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery.
Nat Commun, 15:8709-8709, 2024

PubMed Abstract: The type VI secretion system (T6SS) is a molecular machine utilised by many Gram-negative bacteria to deliver antibacterial toxins into adjacent cells. Here we present the structure of Tse15, a T6SS Rhs effector from the nosocomial pathogen Acinetobacter baumannii. Tse15 forms a triple layered β-cocoon Rhs domain with an N-terminal α-helical clade domain and an unfolded C-terminal toxin domain inside the Rhs cage. Tse15 is cleaved into three domains, through independent auto-cleavage events involving aspartyl protease activity for toxin self-cleavage and a nucleophilic glutamic acid for N-terminal clade cleavage. Proteomic analyses identified that significantly more peptides from the N-terminal clade and toxin domains were secreted than from the Rhs cage, suggesting toxin delivery often occurs without the cage. We propose the clade domain acts as an internal chaperone to mediate toxin tethering to the T6SS machinery. Conservation of the clade domain in other Gram-negative bacteria suggests this may be a common mechanism for delivery.

PubMed: 39379370
DOI: 10.1038/s41467-024-52950-x

実験手法

ELECTRON MICROSCOPY (1.77 Å)