4k19
From Proteopedia
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==The structure of Human Siderocalin bound to the bacterial siderophore fluvibactin== | ==The structure of Human Siderocalin bound to the bacterial siderophore fluvibactin== | ||
| - | <StructureSection load='4k19' size='340' side='right' caption='[[4k19]], [[Resolution|resolution]] 2.74Å' scene=''> | + | <StructureSection load='4k19' size='340' side='right'caption='[[4k19]], [[Resolution|resolution]] 2.74Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4k19]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4k19]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K19 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1OD:(4S,5R)-N,N-BIS{3-[(2,3-DIHYDROXYBENZOYL)AMINO]PROPYL}-2-(2,3-DIHYDROXYPHENYL)-5-METHYL-4,5-DIHYDRO-1,3-OXAZOLE-4-CARBOXAMIDE'>1OD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.74Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1OD:(4S,5R)-N,N-BIS{3-[(2,3-DIHYDROXYBENZOYL)AMINO]PROPYL}-2-(2,3-DIHYDROXYPHENYL)-5-METHYL-4,5-DIHYDRO-1,3-OXAZOLE-4-CARBOXAMIDE'>1OD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k19 OCA], [https://pdbe.org/4k19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k19 RCSB], [https://www.ebi.ac.uk/pdbsum/4k19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k19 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/NGAL_HUMAN NGAL_HUMAN] Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth.<ref>PMID:12453413</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4k19" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Neutrophil gelatinase-associated lipocalin|Neutrophil gelatinase-associated lipocalin]] | *[[Neutrophil gelatinase-associated lipocalin|Neutrophil gelatinase-associated lipocalin]] | ||
| + | *[[Siderocalin 3D structures|Siderocalin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Clifton MC]] |
| - | [[Category: | + | [[Category: Correnti C]] |
| - | [[Category: | + | [[Category: Strong RK]] |
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Current revision
The structure of Human Siderocalin bound to the bacterial siderophore fluvibactin
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