The crystal structure of PD1, a Haemophilus surface fibril domain.

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.

Citation

Jack Wright, Maren Thomsen, Robert Kolodziejczyk, Joshua Ridley, Jessica Sinclair, Glenn Carrington, Birendra Singh, Kristian Riesbeck, Adrian Goldman. The crystal structure of PD1, a Haemophilus surface fibril domain. Acta crystallographica. Section F, Structural biology communications. 2017 Feb 01;73(Pt 2):101-108

Mesh Tags

Substances

PMID: 28177321

search → result