6GBH

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

Summary for 6GBH

• Entry DOI: 10.2210/pdb6gbh/pdb
• Descriptor: Carcinoembryonic antigen-related cell adhesion molecule 1, HopQ, SULFATE ION, ... (4 entities in total)
• Functional Keywords: helicobacter pylori, adhesin, helicobacter outer membrane protein, cell adhesion
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 117160.27

Authors

Moonens, K.,Kruse, T.,Gerhard, M.,Remaut, H. (deposition date: 2018-04-13, release date: 2018-06-27, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.59 Å)