Structural basis for haem piracy from host haemopexin by Haemophilus influenzae

Zambolin, Silvia; Clantin, Bernard; Chami, Mohamed; Hoos, Sylviane; Haouz, Ahmed; Villeret, Vincent; Delepelaire, Philippe

Document type :

Article dans une revue scientifique

DOI :

10.1038/ncomms11590

PMID :

27188378

Permalink :

http://hdl.handle.net/20.500.12210/18303

Title :

Structural basis for haem piracy from host haemopexin by Haemophilus influenzae

Author(s) :

Zambolin, Silvia [Auteur]
Laboratoire de biologie physico-chimique des protéines membranaires [LBPC-PM (UMR_7099)]
Clantin, Bernard [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Chami, Mohamed [Auteur]
Center for Cellular Imaging and Nanoanalytics
Hoos, Sylviane [Auteur]
Biophysique Moléculaire (Plate-forme)
Haouz, Ahmed [Auteur]

Villeret, Vincent [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Delepelaire, Philippe [Auteur]
Laboratoire de biologie physico-chimique des protéines membranaires [LBPC-PM (UMR_7099)]

Journal title :

Nature communications

Abbreviated title :

Nat Commun

Volume number :

Pages :

11590

Publication date :

2016-05-18

ISSN :

2041-1723

English keyword(s) :

blood proteins

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Non spécifiée

ANR Project :

Hème et porphyrine chez des bactéries modèle: des fonctions aux mécanismes

Administrative institution(s) :

CNRS
Université de Lille

Collections :

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Biologie structurale et intégrative

Submission date :

2020-02-12T15:11:26Z
2021-03-26T09:50:55Z
2021-03-26T09:52:04Z

Files

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Except where otherwise noted, this item's license is described as Attribution 3.0 United States

Version	Link	Modification date
3	20.500.12210/18303*	2021-03-26T09:51:38Z
2	20.500.12210/18303.2	2021-03-26T09:31:36Z
1	20.500.12210/18303.1	2020-02-12T15:11:26Z

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Structural basis for haem piracy from host ...

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