5URX

Structure of the contracted type VI secretion system sheath in Myxococcus xanthus

これはPDB形式変換不可エントリーです。

5URX の概要

• エントリーDOI: 10.2210/pdb5urx/pdb
• 関連するPDBエントリー: 5URW
• EMDBエントリー: 8600 8601 8602
• 分子名称: TssB, TssC (2 entities in total)
• 機能のキーワード: t6ss, type iv secretion, protein machine, secretion system, sheath, contractile, protein transport
• 由来する生物種: Myxococcus xanthus; 詳細
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 1335691.55

構造登録者

Chang, Y.-W.,Rettberg, L.A.,Jensen, G.J. (登録日: 2017-02-13, 公開日: 2017-05-10, 最終更新日: 2024-03-13)

主引用文献

Chang, Y.W.,Rettberg, L.A.,Ortega, D.R.,Jensen, G.J.
In vivo structures of an intact type VI secretion system revealed by electron cryotomography.
EMBO Rep., 18:1090-1099, 2017

PubMed Abstract: The type VI secretion system (T6SS) is a versatile molecular weapon used by many bacteria against eukaryotic hosts or prokaryotic competitors. It consists of a cytoplasmic bacteriophage tail-like structure anchored in the bacterial cell envelope via a cytoplasmic baseplate and a periplasmic membrane complex. Rapid contraction of the sheath in the bacteriophage tail-like structure propels an inner tube/spike complex through the target cell envelope to deliver effectors. While structures of purified contracted sheath and purified membrane complex have been solved, because sheaths contract upon cell lysis and purification, no structure is available for the extended sheath. Structural information about the baseplate is also lacking. Here, we use electron cryotomography to directly visualize intact T6SS structures inside cells. Using sub-tomogram averaging, we resolve the structure of the extended sheath and membrane-associated components including the baseplate. Moreover, we identify novel extracellular bacteriophage tail fiber-like antennae. These results provide new structural insights into how the extended sheath prevents premature disassembly and how this sophisticated machine may recognize targets.

PubMed: 28487352
DOI: 10.15252/embr.201744072

実験手法

ELECTRON MICROSCOPY (28 Å)