4YO3

Enteroaggregative Escherichia Coli TssA N-terminal fragment

4YO3 の概要

• エントリーDOI: 10.2210/pdb4yo3/pdb
• 分子名称: TssA (1 entity in total)
• 機能のキーワード: type vi secretion system, transport protein
• 由来する生物種: Escherichia coli 042
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 217513.67

構造登録者

Durand, E.,Zoued, A.,Spinelli, S.,Douzi, B.,Brunet, Y.R.,Bebeacua, C.,Legrand, P.,Journet, L.,Mignot, T.,Cambillau, C.,Cascales, E. (登録日: 2015-03-11, 公開日: 2016-02-17, 最終更新日: 2024-10-16)

主引用文献

Zoued, A.,Durand, E.,Brunet, Y.R.,Spinelli, S.,Douzi, B.,Guzzo, M.,Flaugnatti, N.,Legrand, P.,Journet, L.,Fronzes, R.,Mignot, T.,Cambillau, C.,Cascales, E.
Priming and polymerization of a bacterial contractile tail structure.
Nature, 531:47-52, 2016

PubMed Abstract: Contractile tails are composed of an inner tube wrapped by an outer sheath assembled in an extended, metastable conformation that stores mechanical energy necessary for its contraction. Contraction is used to propel the rigid inner tube towards target cells for DNA or toxin delivery. Although recent studies have revealed the structure of the contractile sheath of the type VI secretion system, the mechanisms by which its polymerization is controlled and coordinated with the assembly of the inner tube remain unknown. Here we show that the starfish-like TssA dodecameric complex interacts with tube and sheath components. Fluorescence microscopy experiments in enteroaggregative Escherichia coli reveal that TssA binds first to the type VI secretion system membrane core complex and then initiates tail polymerization. TssA remains at the tip of the growing structure and incorporates new tube and sheath blocks. On the basis of these results, we propose that TssA primes and coordinates tail tube and sheath biogenesis.

PubMed: 26909579
DOI: 10.1038/nature17182

実験手法

X-RAY DIFFRACTION (3.37 Å)