7Q5P

Structure of VgrG1 from Pseudomonas protegens.

これはPDB形式変換不可エントリーです。

7Q5P の概要

• エントリーDOI: 10.2210/pdb7q5p/pdb
• EMDBエントリー: 13843
• 分子名称: Type VI secretion protein VgrG (1 entity in total)
• 機能のキーワード: bacterial type vi secretion system, toxin, vgrg
• 由来する生物種: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 216240.40

構造登録者

Guenther, P.,Quentin, D.,Ahmad, S.,Sachar, K.,Gatsogiannis, C.,Whitney, J.C.,Raunser, S. (登録日: 2021-11-04, 公開日: 2021-12-15, 最終更新日: 2024-07-17)

主引用文献

Gunther, P.,Quentin, D.,Ahmad, S.,Sachar, K.,Gatsogiannis, C.,Whitney, J.C.,Raunser, S.
Structure of a bacterial Rhs effector exported by the type VI secretion system.
Plos Pathog., 18:e1010182-e1010182, 2022

PubMed Abstract: The type VI secretion system (T6SS) is a widespread protein export apparatus found in Gram-negative bacteria. The majority of T6SSs deliver toxic effector proteins into competitor bacteria. Yet, the structure, function, and activation of many of these effectors remains poorly understood. Here, we present the structures of the T6SS effector RhsA from Pseudomonas protegens and its cognate T6SS spike protein, VgrG1, at 3.3 Å resolution. The structures reveal that the rearrangement hotspot (Rhs) repeats of RhsA assemble into a closed anticlockwise β-barrel spiral similar to that found in bacterial insecticidal Tc toxins and in metazoan teneurin proteins. We find that the C-terminal toxin domain of RhsA is autoproteolytically cleaved but remains inside the Rhs 'cocoon' where, with the exception of three ordered structural elements, most of the toxin is disordered. The N-terminal 'plug' domain is unique to T6SS Rhs proteins and resembles a champagne cork that seals the Rhs cocoon at one end while also mediating interactions with VgrG1. Interestingly, this domain is also autoproteolytically cleaved inside the cocoon but remains associated with it. We propose that mechanical force is required to remove the cleaved part of the plug, resulting in the release of the toxin domain as it is delivered into a susceptible bacterial cell by the T6SS.

PubMed: 34986192
DOI: 10.1371/journal.ppat.1010182

実験手法

ELECTRON MICROSCOPY (3.3 Å)