5LNL
Crystal structure of Hsf 1608-1749 putative domain 1
Summary for 5LNL
| Entry DOI | 10.2210/pdb5lnl/pdb |
| Descriptor | Hsf (1 entity in total) |
| Functional Keywords | haemophilus influenzae, trimeric autotransporter, adhesin, cell adhesion |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 9 |
| Total formula weight | 143644.35 |
| Authors | Thomsen, M.,Wright, J.,Ridley, J.,Goldman, A. (deposition date: 2016-08-05, release date: 2017-02-15, Last modification date: 2024-01-10) |
| Primary citation | Wright, J.,Thomsen, M.,Kolodziejczyk, R.,Ridley, J.,Sinclair, J.,Carrington, G.,Singh, B.,Riesbeck, K.,Goldman, A. The crystal structure of PD1, a Haemophilus surface fibril domain. Acta Crystallogr F Struct Biol Commun, 73:101-108, 2017 Cited by PubMed Abstract: The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel `hairpin-like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high-resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 Å resolution. The structure corrects the previous domain annotation by revealing the presence of an unexpected N-terminal TrpRing domain. PD1 represents the first Hsf domain to be solved, and thus paves the way for further research on the `hairpin-like' hypothesis. PubMed: 28177321DOI: 10.1107/S2053230X17001406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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