Download MendeleyThe crystal structure of PD1, a Haemophilus surface fibril domain.
Wright, J., Thomsen, M., Kolodziejczyk, R., Ridley, J., Sinclair, J., Carrington, G., Singh, B., Riesbeck, K., Goldman, A.(2017) Acta Crystallogr F Struct Biol Commun 73: 101-108
- PubMed: 28177321
- DOI: https://doi.org/10.1107/S2053230X17001406
- Primary Citation of Related Structures:
5LNL - 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.
Organizational Affiliation:
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
