5Y9G

Crystal structure of Salmonella SafD adhesin

5Y9G の概要

• エントリーDOI: 10.2210/pdb5y9g/pdb
• 分子名称: Pilin structural protein SafD,Pilus assembly protein (2 entities in total)
• 機能のキーワード: host recognition, biofilm formation, salmonella atypical fimbriae, poly-adhesive activity, self-associating oligomerization, cell adhesion
• 由来する生物種: Salmonella enteritidis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32569.73

構造登録者

Zeng, L.H.,Zhang, L.,Wang, P.R.,Meng, G. (登録日: 2017-08-25, 公開日: 2017-11-15, 最終更新日: 2023-11-22)

主引用文献

Zeng, L.H.,Zhang, L.,Wang, P.R.,Meng, G.
Structural basis of host recognition and biofilm formation by Salmonella Saf pili
Elife, 6:-, 2017

PubMed Abstract: Pili are critical in host recognition, colonization and biofilm formation during bacterial infection. Here, we report the crystal structures of SafD- and SafD-SafA-SafA (SafDAA-) in Saf pili. Cell adherence assays show that SafD and SafA are both required for host recognition, suggesting a poly-adhesive mechanism for Saf pili. Moreover, the SafDAA- structure, as well as SAXS characterization, reveals an unexpected inter-molecular oligomerization, prompting the investigation of Saf-driven self-association in biofilm formation. The bead/cell aggregation and biofilm formation assays are used to demonstrate the novel function of Saf pili. Structure-based mutants targeting the inter-molecular hydrogen bonds and complementary architecture/surfaces in SafDAA- dimers significantly impaired the Saf self-association activity and biofilm formation. In summary, our results identify two novel functions of Saf pili: the poly-adhesive and self-associating activities. More importantly, Saf-Saf structures and functional characterizations help to define a pili-mediated inter-cellular oligomerizaiton mechanism for bacterial aggregation, colonization and ultimate biofilm formation.

PubMed: 29125121
DOI: 10.7554/eLife.28619

実験手法

X-RAY DIFFRACTION (2.2 Å)