6XZC

CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis

6XZC の概要

• エントリーDOI: 10.2210/pdb6xzc/pdb
• 関連するPDBエントリー: 3J83
• EMDBエントリー: 10658
• 分子名称: ESX-1 secretion-associated protein EspB (1 entity in total)
• 機能のキーワード: m. tuberculosis, esx-1, type vii secretion system, espb, rv3881c, esxa, cfp10, esat-6, transport protein
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 333462.69

構造登録者

Piton, J.,Pojer, F.,Wakatsuki, S.,Gati, C.,Cole, S.T. (登録日: 2020-02-03, 公開日: 2020-06-17, 最終更新日: 2024-05-22)

主引用文献

Piton, J.,Pojer, F.,Wakatsuki, S.,Gati, C.,Cole, S.T.
High resolution CryoEM structure of the ring-shaped virulence factor EspB fromMycobacterium tuberculosis.
J Struct Biol X, 4:100029-100029, 2020

PubMed Abstract: The EspB protein of is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of EspB by cryo-electron microscopic examination of single particles have been thwarted by severe orientation bias of the particles. This was overcome by using detergent as a surfactant thereby allowing reconstruction of the EspB structure at 3.37 Å resolution. The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 Å x 90 Å and a central channel of 45 Å diameter whereas the C-terminal domain was unstructured. New atomic insight was obtained into the helical packing required for protomer interactions and the overall electrostatic potential. The external surface is electronegatively charged while the channel is lined with electropositive patches. EspB thus has many features of a pore-like transport protein that might allow the passage of an ESX-1 substrate such as the 35 Å diameter EsxA-EsxB heterodimer or B-form DNA consistent with its proposed role in DNA uptake.

PubMed: 32875288
DOI: 10.1016/j.yjsbx.2020.100029

実験手法

ELECTRON MICROSCOPY (3.37 Å)