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Structural basis for haem piracy from host haemopexin by Haemophilus influenzae

Abstract : Haemophilus influenzae is an obligate human commensal/pathogen that requires haem for survival and can acquire it from several host haemoproteins, including haemopexin. The haem transport system from haem-haemopexin consists of HxuC, a haem receptor, and the two-partner-secretion system HxuB/HxuA. HxuA, which is exposed at the cell surface, is strictly required for haem acquisition from haemopexin. HxuA forms complexes with haem-haemopexin, leading to haem release and its capture by HxuC. The key question is how HxuA liberates haem from haemopexin. Here, we solve crystal structures of HxuA alone, and HxuA in complex with the N-terminal domain of haemopexin. A rational basis for the release of haem from haem-haemopexin is derived from both in vivo and in vitro studies. HxuA acts as a wedge that destabilizes the two-domains structure of haemopexin with a mobile loop on HxuA that favours haem ejection by redirecting key residues in the haem-binding pocket of haemopexin.
Keywords : blood proteins
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https://hal.univ-lille.fr/hal-03182142
Contributeur : Lilloa Université de Lille <>
Soumis le : vendredi 26 mars 2021 - 10:51:10
Dernière modification le : lundi 21 juin 2021 - 14:32:05
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Silvia Zambolin, Bernard Clantin, Mohamed Chami, Sylviane Hoos, Ahmed Haouz, et al.. Structural basis for haem piracy from host haemopexin by Haemophilus influenzae. Nature Communications, Nature Publishing Group, 2016, 7, pp.11590. ⟨10.1038/ncomms11590⟩. ⟨hal-03182142⟩

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