5lnl | pdb_00005lnl

Crystal structure of Hsf 1608-1749 putative domain 1

spinqualitylabelsall models 5lnl, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lnl is a 9 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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. The 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 Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):101-108. doi:, 10.1107/S2053230X17001406. Epub 2017 Jan 31. PMID:28177321 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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