期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 431, 期 10, 页码 1956-1965出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.03.029
关键词
single-particle cryo-EM; pore-forming toxins; gastric cancer
资金
- National Institutes of Health [AI039657, CA116087, T32CA119925, T32GM08320, R35GM118089, F31A1112324]
- Department of Veterans Affairs [1I01BX004447]
- U-M LSI IT
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 cryoelectron microscopy, we have determined low-resolution structures of a VacA dodecamer and heptamer, as well as a 3.8-angstrom 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. (C) 2019 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据