7K7K
Structure of the EPEC type III secretion injectisome EspA filament
7K7K の概要
| エントリーDOI | 10.2210/pdb7k7k/pdb |
| EMDBエントリー | 22701 |
| 分子名称 | Translocon EspA (1 entity in total) |
| 機能のキーワード | transport, filament, secretion system, protein transport |
| 由来する生物種 | Escherichia coli O127:H6 (strain E2348/69 / EPEC) |
| タンパク質・核酸の鎖数 | 28 |
| 化学式量合計 | 573518.71 |
| 構造登録者 | Lyons, B.J.E.,Atkinson, C.E.,Strynadka, N.C.J. (登録日: 2020-09-23, 公開日: 2020-12-30, 最終更新日: 2024-03-06) |
| 主引用文献 | Lyons, B.J.E.,Atkinson, C.E.,Deng, W.,Serapio-Palacios, A.,Finlay, B.B.,Strynadka, N.C.J. Cryo-EM structure of the EspA filament from enteropathogenic Escherichia coli: Revealing the mechanism of effector translocation in the T3SS. Structure, 29:479-, 2021 Cited by PubMed Abstract: The type III secretion system (T3SS) is a virulence mechanism employed by Gram-negative pathogens. The T3SS forms a proteinaceous channel that projects a needle into the extracellular medium where it interacts with the host cell to deliver virulence factors. Enteropathogenic Escherichia coli (EPEC) is unique in adopting a needle extension to the T3SS-a filament formed by EspA-which is absolutely required for efficient colonization of the gut. Here, we describe the cryoelectron microscopy structure of native EspA filaments from EPEC at 3.6-Å resolution. Within the filament, positively charged residues adjacent to a hydrophobic groove line the lumen of the filament in a spiral manner, suggesting a mechanism of substrate translocation mediated via electrostatics. Using structure-guided mutagenesis, in vivo studies corroborate the role of these residues in secretion and translocation function. The high-resolution structure of the EspA filament could aid in structure-guided drug design of antivirulence therapeutics. PubMed: 33453150DOI: 10.1016/j.str.2020.12.009 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.56 Å) |
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