Structural basis for haem piracy from host haemopexin by Haemophilus influenzae - Université de Lille Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2016

Structural basis for haem piracy from host haemopexin by Haemophilus influenzae

Résumé

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.

Mots clés

Fichier principal
Vignette du fichier
ncomms11590.pdf (1.97 Mo) Télécharger le fichier
Origine Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-03182142 , version 1 (26-03-2021)

Licence

Identifiants

Citer

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, 2016, 7, pp.11590. ⟨10.1038/ncomms11590⟩. ⟨hal-03182142⟩
55 Consultations
64 Téléchargements

Altmetric

Partager

Gmail Mastodon Facebook X LinkedIn More