6ODY

Cryo-EM structure of Helicobacter pylori VacA hexamer

6ODY の概要

• エントリーDOI: 10.2210/pdb6ody/pdb
• EMDBエントリー: 20024
• 分子名称: Vacuolating cytotoxin autotransporter (1 entity in total)
• 機能のキーワード: vaca, toxin
• 由来する生物種: Helicobacter pylori; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 422355.47

構造登録者

Erwin, A.L.,Cover, T.L.,Ohi, M.D. (登録日: 2019-03-27, 公開日: 2019-09-25, 最終更新日: 2024-10-16)

主引用文献

Su, M.,Erwin, A.L.,Campbell, A.M.,Pyburn, T.M.,Salay, L.E.,Hanks, J.L.,Lacy, D.B.,Akey, D.L.,Cover, T.L.,Ohi, M.D.
Cryo-EM Analysis Reveals Structural Basis of Helicobacter pylori VacA Toxin Oligomerization.
J.Mol.Biol., 431:1956-1965, 2019

PubMed Abstract: Helicobacter pylori colonizes the human stomach and contributes to the development of gastric cancer and peptic ulcer disease. H. pylori secretes a pore-forming toxin called vacuolating cytotoxin A (VacA), which contains two domains (p33 and p55) and assembles into oligomeric structures. Using single-particle cryo-electron microscopy, we have determined low-resolution structures of a VacA dodecamer and heptamer, as well as a 3.8-Å structure of the VacA hexamer. These analyses show that VacA p88 consists predominantly of a right-handed beta-helix that extends from the p55 domain into the p33 domain. We map the regions of p33 and p55 involved in hexamer assembly, model how interactions between protomers support heptamer formation, and identify surfaces of VacA that likely contact membrane. This work provides structural insights into the process of VacA oligomerization and identifies regions of VacA protomers that are predicted to contact the host cell surface during channel formation.

PubMed: 30954575
DOI: 10.1016/j.jmb.2019.03.029

実験手法

ELECTRON MICROSCOPY (3.8 Å)