Structural basis for haem piracy from host haemopexin by Haemophilus influenzae

Zambolin, Silvia and Clantin, Bernard and Chami, Mohamed and Hoos, Sylviane and Haouz, Ahmed and Villeret, Vincent and Delepelaire, Philippe. (2016) Structural basis for haem piracy from host haemopexin by Haemophilus influenzae. Nature communications, 7. p. 11590.

Full text not available from this repository.

Official URL: https://edoc.unibas.ch/78625/

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:05 Oct 2020 06:41
Deposited On:05 Oct 2020 06:41

Repository Staff Only: item control page