6SKI

The Tle hydrolase bound to the TTR domain of the VgrG spike of the Type 6 secretion system

6SKI の概要

• エントリーDOI: 10.2210/pdb6ski/pdb
• EMDBエントリー: 10225
• 分子名称: Putative type VI secretion protein (2 entities in total)
• 機能のキーワード: lipase, effector, toxin, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 155079.97

構造登録者

Rapisarda, C.,Fronzes, R. (登録日: 2019-08-15, 公開日: 2020-04-15, 最終更新日: 2024-05-22)

主引用文献

Flaugnatti, N.,Rapisarda, C.,Rey, M.,Beauvois, S.G.,Nguyen, V.A.,Canaan, S.,Durand, E.,Chamot-Rooke, J.,Cascales, E.,Fronzes, R.,Journet, L.
Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike.
Embo J., 39:e104129-e104129, 2020

PubMed Abstract: The bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: the contraction of a sheath structure pushes a tube topped by a spike into target cells. Effectors are loaded onto the spike or confined into the tube. In enteroaggregative Escherichia coli, the Tle1 phospholipase binds the C-terminal extension of the VgrG trimeric spike. Here, we purify the VgrG-Tle1 complex and show that a VgrG trimer binds three Tle1 monomers and inhibits their activity. Using covalent cross-linking coupled to high-resolution mass spectrometry, we provide information on the sites of contact and further identify the requirement for a Tle1 N-terminal secretion sequence in complex formation. Finally, we report the 2.6-Å-resolution cryo-electron microscopy tri-dimensional structure of the (VgrG) -(Tle1) complex revealing how the effector binds its cargo, and how VgrG inhibits Tle1 phospholipase activity. The inhibition of Tle1 phospholipase activity once bound to VgrG suggests that Tle1 dissociation from VgrG is required upon delivery.

PubMed: 32350888
DOI: 10.15252/embj.2019104129

実験手法

ELECTRON MICROSCOPY (2.6 Å)