3J83

Heptameric EspB Rosetta model guided by EM density

3J83 の概要

• エントリーDOI: 10.2210/pdb3j83/pdb
• EMDBエントリー: 6120
• 分子名称: ESX-1 secretion-associated protein EspB (1 entity in total)
• 機能のキーワード: protein binding
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 276882.59

構造登録者

Solomonson, M.,DiMaio, F.,Strynadka, N.C.J. (登録日: 2014-09-30, 公開日: 2015-03-11, 最終更新日: 2024-02-21)

主引用文献

Solomonson, M.,Setiaputra, D.,Makepeace, K.A.,Lameignere, E.,Petrotchenko, E.V.,Conrady, D.G.,Bergeron, J.R.,Vuckovic, M.,DiMaio, F.,Borchers, C.H.,Yip, C.K.,Strynadka, N.C.
Structure of EspB from the ESX-1 Type VII Secretion System and Insights into its Export Mechanism.
Structure, 23:571-583, 2015

PubMed Abstract: Mycobacterium tuberculosis (Mtb) uses the ESX-1 type VII secretion system to export virulence proteins across its lipid-rich cell wall, which helps permeabilize the host's macrophage phagosomal membrane, facilitating the escape and cell-to-cell spread of Mtb. ESX-1 membranolytic activity depends on a set of specialized secreted Esp proteins, the structure and specific roles of which are not currently understood. Here, we report the X-ray and electron microscopic structures of the ESX-1-secreted EspB. We demonstrate that EspB adopts a PE/PPE-like fold that mediates oligomerization with apparent heptameric symmetry, generating a barrel-shaped structure with a central pore that we propose contributes to the macrophage killing functions of EspB. Our structural data also reveal unexpected direct interactions between the EspB bipartite secretion signal sequence elements that form a unified aromatic surface. These findings provide insight into how specialized proteins encoded within the ESX-1 locus are targeted for secretion, and for the first time indicate an oligomerization-dependent role for Esp virulence factors.

PubMed: 25684576
DOI: 10.1016/j.str.2015.01.002

実験手法

ELECTRON MICROSCOPY (30 Å)