Structural basis for haem piracy from host ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Structural basis for haem piracy from host haemopexin by Haemophilus influenzae
Auteur(s) :
Zambolin, Silvia [Auteur]
Clantin, Bernard [Auteur]
Chami, Mohamed [Auteur]
Hoos, Sylviane [Auteur]
Haouz, Ahmed [Auteur]
Villeret, Vincent [Auteur]
Delepelaire, Philippe [Auteur]
Clantin, Bernard [Auteur]
Chami, Mohamed [Auteur]
Hoos, Sylviane [Auteur]
Haouz, Ahmed [Auteur]
Villeret, Vincent [Auteur]
Delepelaire, Philippe [Auteur]
Titre de la revue :
Nature communications
Nom court de la revue :
Nat Commun
Numéro :
7
Pagination :
11590
Date de publication :
2016-05-18
ISSN :
2041-1723
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:26Z