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| | <StructureSection load='5ec6' size='340' side='right'caption='[[5ec6]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5ec6' size='340' side='right'caption='[[5ec6]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ec6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Kingella_denitrificans_atcc_33394 Kingella denitrificans atcc 33394]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EC6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ec6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kingella_denitrificans_ATCC_33394 Kingella denitrificans ATCC 33394]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EC6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=END:1,6 5,9 8,12 11,16-TETRAANHYDRO-2,3,4,10,13,14-HEXADEOXY-D-GLYCERO-D-ALLO-D-GULO-HEPTADECA-2,13-DIENITOL'>END</scene></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=5ec6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ec6 OCA], [https://pdbe.org/5ec6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ec6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ec6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ec6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF9098_0447 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=888741 Kingella denitrificans ATCC 33394])</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=5ec6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ec6 OCA], [http://pdbe.org/5ec6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ec6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ec6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ec6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F0EX68_9NEIS F0EX68_9NEIS] |
| | <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: Kingella denitrificans atcc 33394]] | + | [[Category: Kingella denitrificans ATCC 33394]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garnett, J A]] | + | [[Category: Garnett JA]] |
| - | [[Category: Hare, S A]] | + | [[Category: Hare SA]] |
| - | [[Category: Wong, C T]] | + | [[Category: Wong CT]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Lipoprotein]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Outer membrane]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
Function
F0EX68_9NEIS
Publication Abstract from PubMed
The Neisseriaceae family of bacteria causes a range of diseases including meningitis, septicaemia, gonorrhoea and endocarditis, and extracts haem from haemoglobin as an important iron source within the iron-limited environment of its human host. Herein we report crystal structures of apo- and haemoglobin-bound HpuA, an essential component of this haem import system. The interface involves long loops on the bacterial receptor that present hydrophobic side chains for packing against the surface of haemoglobin. Interestingly, our structural and biochemical analyses of Kingella denitrificans and Neisseria gonorrhoeae HpuA mutants, although validating the interactions observed in the crystal structure, show how Neisseriaceae have the fascinating ability to diversify functional sequences and yet retain the haemoglobin binding function. Our results present the first description of HpuA's role in direct binding of haemoglobin.
Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family.,Wong CT, Xu Y, Gupta A, Garnett JA, Matthews SJ, Hare SA Nat Commun. 2015 Dec 16;6:10172. doi: 10.1038/ncomms10172. PMID:26671256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wong CT, Xu Y, Gupta A, Garnett JA, Matthews SJ, Hare SA. Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family. Nat Commun. 2015 Dec 16;6:10172. doi: 10.1038/ncomms10172. PMID:26671256 doi:http://dx.doi.org/10.1038/ncomms10172
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