6GBG

Helicobacter pylori adhesin HopQ type I bound to the N-terminal domain of human CEACAM1

6GBG の概要

• エントリーDOI: 10.2210/pdb6gbg/pdb
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 1, Outer membrane protein, BROMIDE ION, ... (4 entities in total)
• 機能のキーワード: helicobacter pylori, adhesin, helicobacter outer membrane protein, cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57418.48

構造登録者

Moonens, K.,Kruse, T.,Gerhard, M.,Remaut, H. (登録日: 2018-04-13, 公開日: 2018-06-27, 最終更新日: 2024-11-20)

主引用文献

Moonens, K.,Hamway, Y.,Neddermann, M.,Reschke, M.,Tegtmeyer, N.,Kruse, T.,Kammerer, R.,Mejias-Luque, R.,Singer, B.B.,Backert, S.,Gerhard, M.,Remaut, H.
Helicobacter pyloriadhesin HopQ disruptstransdimerization in human CEACAMs.
EMBO J., 37:-, 2018

PubMed Abstract: The human gastric pathogen is a major causative agent of gastritis, peptic ulcer disease, and gastric cancer. As part of its adhesive lifestyle, the bacterium targets members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family by the conserved outer membrane adhesin HopQ. The HopQ-CEACAM1 interaction is associated with inflammatory responses and enables the intracellular delivery and phosphorylation of the CagA oncoprotein via a yet unknown mechanism. Here, we generated crystal structures of HopQ isotypes I and II bound to the N-terminal domain of human CEACAM1 (C1ND) and elucidated the structural basis of specificity toward human CEACAM receptors. Both HopQ alleles target the β-strands G, F, and C of C1ND, which form the dimerization interface in homo- and heterophilic CEACAM interactions. Using SAXS, we show that the HopQ ectodomain is sufficient to induce C1ND monomerization and thus providing a route to influence CEACAM-mediated cell adherence and signaling events.

PubMed: 29858229
DOI: 10.15252/embj.201798665

実験手法

X-RAY DIFFRACTION (2.8 Å)