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4RT6

Structure of a complex between hemopexin and hemopexin binding protein

Summary for 4RT6
Entry DOI10.2210/pdb4rt6/pdb
Related1QHU 1QJS 4I84 4RM6
DescriptorHeme/hemopexin-binding protein, Hemopexin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsbeta-helix; beta-propeller domain, interaction of hxua with hemopexin enables heme release from hemopexin, outer membrane, protein binding
Biological sourceHaemophilus influenzae Rd KW20
More
Total number of polymer chains2
Total formula weight121488.15
Authors
Zambolin, S.,Clantin, B.,Haouz, A.,Villeret, V.,Delepelaire, P. (deposition date: 2014-11-13, release date: 2016-05-18, Last modification date: 2024-10-30)
Primary citationZambolin, S.,Clantin, B.,Chami, M.,Hoos, S.,Haouz, A.,Villeret, V.,Delepelaire, P.
Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.
Nat Commun, 7:11590-11590, 2016
Cited by
PubMed 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.
PubMed: 27188378
DOI: 10.1038/ncomms11590
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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