4FZQ

Crystal structure of HP0197-G5

4FZQ の概要

• エントリーDOI: 10.2210/pdb4fzq/pdb
• 関連するPDBエントリー: 4FZ4
• 分子名称: Uncharacterized protein conserved in bacteria (2 entities in total)
• 機能のキーワード: immune system
• 由来する生物種: Streptococcus suis (HP0197-G5)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 52680.37

構造登録者

Yuan, Z.,Yan, X. (登録日: 2012-07-07, 公開日: 2012-12-05, 最終更新日: 2024-03-20)

主引用文献

Yuan, Z.Z.,Yan, X.J.,Zhang, A.D.,Chen, B.,Shen, Y.Q.,Jin, M.L.
Molecular mechanism by which surface antigen HP0197 mediates host cell attachment in the pathogenic bacteria Streptococcus suis
J.Biol.Chem., 288:956-963, 2013

PubMed Abstract: Streptococcus suis, one of the most important and prevalent pathogens in swine, presents a major challenge to global public health. HP0197 is an S. suis surface antigen that was previously identified by immunoproteomics and can bind to the host cell surface. Here, we investigated the interaction between HP0197 and the host cell surface glycosaminoglycans (GAGs) using indirect immunofluorescence and cell adhesion inhibition assays. In addition, we determined that a novel 18-kDa domain in the N-terminal region of HP0197 functions as the GAG-binding domain. We then solved the three-dimensional structures of the N-terminal 18-kDa and C-terminal G5 domains using x-ray crystallography. Based on this structural information, the GAG-binding sites in HP0197 were predicted and subsequently verified using site-directed mutagenesis and indirect immunofluorescence. The results indicate that the positively charged residues on the exposed surface of the 18-kDa domain, which are primarily lysines, likely play a critical role in the HP0197-heparin interaction that mediates bacterium-host cell adhesion. Understanding this molecular mechanism may provide a basis for the development of effective drugs and therapeutic strategies for treating streptococcal infections.

PubMed: 23184929
DOI: 10.1074/jbc.M112.388686

実験手法

X-RAY DIFFRACTION (2.5 Å)