5LNL

Crystal structure of Hsf 1608-1749 putative domain 1

5LNL の概要

• エントリーDOI: 10.2210/pdb5lnl/pdb
• 分子名称: Hsf (1 entity in total)
• 機能のキーワード: haemophilus influenzae, trimeric autotransporter, adhesin, cell adhesion
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 143644.35

構造登録者

Thomsen, M.,Wright, J.,Ridley, J.,Goldman, A. (登録日: 2016-08-05, 公開日: 2017-02-15, 最終更新日: 2024-01-10)

主引用文献

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

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: 28177321
DOI: 10.1107/S2053230X17001406

実験手法

X-RAY DIFFRACTION (3.3 Å)