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| | <StructureSection load='4rt6' size='340' side='right'caption='[[4rt6]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4rt6' size='340' side='right'caption='[[4rt6]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rt6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haein Haein] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RT6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rt6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RT6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rm6|4rm6]], [[4i84|4i84]], [[1qhu|1qhu]], [[1qjs|1qjs]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt6 OCA], [https://pdbe.org/4rt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rt6 RCSB], [https://www.ebi.ac.uk/pdbsum/4rt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rt6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hxuA, HI_0264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 HAEIN])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rt6 OCA], [http://pdbe.org/4rt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rt6 RCSB], [http://www.ebi.ac.uk/pdbsum/4rt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rt6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HXUA1_HAEIN HXUA1_HAEIN]] Binds heme/hemopexin complexes. [[http://www.uniprot.org/uniprot/HEMO_RABIT HEMO_RABIT]] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. | + | [https://www.uniprot.org/uniprot/HXUA1_HAEIN HXUA1_HAEIN] Binds heme/hemopexin complexes. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haein]] | + | [[Category: Haemophilus influenzae Rd KW20]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Clantin, B]] | + | [[Category: Clantin B]] |
| - | [[Category: Delepelaire, P]] | + | [[Category: Delepelaire P]] |
| - | [[Category: Haouz, A]] | + | [[Category: Haouz A]] |
| - | [[Category: Villeret, V]] | + | [[Category: Villeret V]] |
| - | [[Category: Zambolin, S]] | + | [[Category: Zambolin S]] |
| - | [[Category: Beta-helix]]
| + | |
| - | [[Category: Beta-propeller domain]]
| + | |
| - | [[Category: Interaction of hxua with hemopexin enables heme release from hemopexin]]
| + | |
| - | [[Category: Outer membrane]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zambolin 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. 2016 May 18;7:11590. doi: 10.1038/ncomms11590. PMID:27188378 doi:http://dx.doi.org/10.1038/ncomms11590
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