4rt6

Structure of a complex between hemopexin and hemopexin binding protein

spinqualitylabelsall models 4rt6, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rt6 is a 2 chain structure with sequence from Haemophilus influenzae Rd KW20 and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HXUA1_HAEIN Binds heme/hemopexin complexes. Publication Abstract from PubMed 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. Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.,Zambolin S, Clantin B, Chami M, Hoos S, Haouz A, Villeret V, Delepelaire P Nat Commun. 2016 May 18;7:11590. doi: 10.1038/ncomms11590. PMID:27188378 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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