3SYJ
Crystal structure of the Haemophilus influenzae Hap adhesin
Summary for 3SYJ
| Entry DOI | 10.2210/pdb3syj/pdb |
| Descriptor | Adhesion and penetration protein autotransporter (2 entities in total) |
| Functional Keywords | bacterial aggregation and biofilm formation, self-associating autotransporter (saat), oligomerization, beta helix fold, membrane, cell adhesion |
| Biological source | Haemophilus influenzae |
| Cellular location | Adhesion and penetration protein autotransporter: Periplasm . Adhesion and penetration protein: Secreted. Adhesion and penetration protein translocator: Cell outer membrane ; Multi-pass membrane protein : P45387 |
| Total number of polymer chains | 1 |
| Total formula weight | 112138.53 |
| Authors | Meng, G. (deposition date: 2011-07-18, release date: 2011-08-24, Last modification date: 2024-10-16) |
| Primary citation | Meng, G.,Spahich, N.,Kenjale, R.,Waksman, G.,St Geme III, J.W. Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation Embo J., 30:3864-3874, 2011 Cited by PubMed Abstract: Bacterial biofilms are complex microbial communities that are common in nature and are being recognized increasingly as an important determinant of bacterial virulence. However, the structural determinants of bacterial aggregation and eventual biofilm formation have been poorly defined. In Gram-negative bacteria, a major subgroup of extracellular proteins called self-associating autotransporters (SAATs) can mediate cell-cell adhesion and facilitate biofilm formation. In this study, we used the Haemophilus influenzae Hap autotransporter as a prototype SAAT to understand how bacteria associate with each other. The crystal structure of the H. influenzae Hap(S) passenger domain (harbouring the SAAT domain) was determined to 2.2 Å by X-ray crystallography, revealing an unprecedented intercellular oligomerization mechanism for cell-cell interaction. The C-terminal SAAT domain folds into a triangular-prism-like structure that can mediate Hap-Hap dimerization and higher degrees of multimerization through its F1-F2 edge and F2 face. The intercellular multimerization can give rise to massive buried surfaces that are required for overcoming the repulsive force between cells, leading to bacterial cell-cell interaction and formation of complex microcolonies. PubMed: 21841773DOI: 10.1038/emboj.2011.279 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
