5H3X

The structure of the N-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)

5H3X の概要

• エントリーDOI: 10.2210/pdb5h3x/pdb
• 関連するPDBエントリー: 5H3W
• 分子名称: Fibronectin/fibrinogen binding protein (2 entities in total)
• 機能のキーワード: fibronectin-binding property, cell adhesion
• 由来する生物種: Streptococcus suis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30597.45

構造登録者

MokiMusyoki, A.,Qi, J.,Gao, G.F. (登録日: 2016-10-27, 公開日: 2016-11-16, 最終更新日: 2024-03-20)

主引用文献

Musyoki, A.M.,Shi, Z.,Xuan, C.,Lu, G.,Qi, J.,Gao, F.,Zheng, B.,Zhang, Q.,Li, Y.,Haywood, J.,Liu, C.,Yan, J.,Shi, Y.,Gao, G.F.
Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis
Proc. Natl. Acad. Sci. U.S.A., 113:13869-13874, 2016

PubMed Abstract: The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 Å, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via β1 integrin receptors to induce chemokine production.

PubMed: 27834729
DOI: 10.1073/pnas.1608406113

実験手法

X-RAY DIFFRACTION (2.1 Å)