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.
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Jack
J
Wright
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Maren
M
Thomsen
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Robert
R
Kolodziejczyk
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Joshua
J
Ridley
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Jessica
J
Sinclair
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Glenn
G
Carrington
Department of Clinical Microbiology, Lund University, Jan Waldenströms gata 59, SE-205 02 Malmö, Sweden.
Birendra
B
Singh
Department of Clinical Microbiology, Lund University, Jan Waldenströms gata 59, SE-205 02 Malmö, Sweden.
Kristian
K
Riesbeck
Astbury Centre for Structural Molecular Biology, School of Biomedical Science, University of Leeds, Leeds LS2 9JT, England.
Adrian
A
Goldman
D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006193:Haemophilus influenzae / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040681:Structural Homology, Protein
D018829:Adhesins, Bacterial; C429644:Hia adhesin; C102673:Hsf protein, bacteria; D011994:Recombinant Proteins
Haemophilus influenzae; Haemophilus surface fibril; Hsf putative domain 1; adhesin; cell adhesion; trimeric autotransporter