6AW2

Crystal structure of the HopQ-CEACAM1 complex

6AW2 の概要

• エントリーDOI: 10.2210/pdb6aw2/pdb
• 分子名称: Carcinoembryonic antigen-related cell adhesion molecule 1, HopQ (3 entities in total)
• 機能のキーワード: 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: 59129.05

構造登録者

Bonsor, D.A.,Sundberg, E.J. (登録日: 2017-09-05, 公開日: 2018-05-16, 最終更新日: 2023-10-04)

主引用文献

Bonsor, D.A.,Zhao, Q.,Schmidinger, B.,Weiss, E.,Wang, J.,Deredge, D.,Beadenkopf, R.,Dow, B.,Fischer, W.,Beckett, D.,Wintrode, P.L.,Haas, R.,Sundberg, E.J.
TheHelicobacter pyloriadhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA.
EMBO J., 37:-, 2018

PubMed Abstract: infects half of the world's population, and strains that encode the type IV secretion system for injection of the oncoprotein CagA into host gastric epithelial cells are associated with elevated levels of cancer. CagA translocation into host cells is dependent on interactions between the adhesin protein HopQ and human CEACAMs. Here, we present high-resolution structures of several HopQ-CEACAM complexes and CEACAMs in their monomeric and dimeric forms establishing that HopQ uses a coupled folding and binding mechanism to engage the canonical CEACAM dimerization interface for CEACAM recognition. By combining mutagenesis with biophysical and functional analyses, we show that the modes of CEACAM recognition by HopQ and CEACAMs themselves are starkly different. Our data describe precise molecular mechanisms by which microbes exploit host CEACAMs for infection and enable future development of novel oncoprotein translocation inhibitors and -specific antimicrobial agents.

PubMed: 29724755
DOI: 10.15252/embj.201798664

実験手法

X-RAY DIFFRACTION (2.68 Å)