5Y9H
Crystal structure of SafDAA-dsc complex
Summary for 5Y9H
| Entry DOI | 10.2210/pdb5y9h/pdb |
| Related | 5Y9G |
| Descriptor | SafD,Putative outer membrane protein,Putative outer membrane protein,Putative outer membrane protein (2 entities in total) |
| Functional Keywords | host recognition, biofilm formation, salmonella atypical fimbriae, poly-adhesive activity, self-associating oligomerization, cell adhesion |
| Biological source | Salmonella typhimurium More |
| Total number of polymer chains | 3 |
| Total formula weight | 150192.92 |
| Authors | Zeng, L.H.,Zhang, L.,Wang, P.R.,Meng, G. (deposition date: 2017-08-25, release date: 2017-11-15, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 29125121DOI: 10.7554/eLife.28619 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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