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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2w0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0O FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2w0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dat|1dat]], [[1gwg|1gwg]], [[2v2j|2v2j]], [[1xz3|1xz3]], [[1hrs|1hrs]], [[2v2i|2v2i]], [[2v2o|2v2o]], [[2v2m|2v2m]], [[1ier|1ier]], [[2gyd|2gyd]], [[2v2l|2v2l]], [[2v2s|2v2s]], [[2v2p|2v2p]], [[2v2r|2v2r]], [[1aew|1aew]], [[2v2n|2v2n]], [[1xz1|1xz1]], [[1ies|1ies]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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'>[https://proteopedia.org/fgij/fg.htm?mol=2w0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0o OCA], [https://pdbe.org/2w0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0o RCSB], [https://www.ebi.ac.uk/pdbsum/2w0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0o ProSAT]</span></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=2w0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0o OCA], [https://pdbe.org/2w0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0o RCSB], [https://www.ebi.ac.uk/pdbsum/2w0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
| + | [https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Declercq, J P]] | + | [[Category: De Val N]] |
| - | [[Category: Val, N De]]
| + | [[Category: Declercq JP]] |
| - | [[Category: Acetylation]] | + | |
| - | [[Category: Apoferritin]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron storage]]
| + | |
| - | [[Category: Metal transport]]
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| - | [[Category: Metal-binding]]
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| Structural highlights
Function
FRIL_HORSE Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
There are extensive structural similarities between eukaryotic and prokaryotic ferritins. However, there is one essential difference between these two types of ferritins: bacterioferritins contain haem whereas eukaryotic ferritins are considered to be non-haem proteins. In vitro experiments had shown that horse spleen apoferritin or recombinant horse L chain apoferritins, when co-crystallised with haemin, undergoes demetallation of the porphyrin. In the present study a cofactor has been isolated directly from horse spleen apoferritin and from crystals of the mutant horse L chain apoferritin (E53Q, E56Q, E57Q, E60Q and R59M) which had been co-crystallised with haemin. In both cases the HPLC/ESI-MS results confirm that the cofactor is a N-ethylprotoporphyrin IX. Crystal structures of wild type L chain horse apoferritin and its three mutants co-crystallised with haemin have been determined to high resolution and in all cases a metal-free molecule derived from haemin was found in the hydrophobic pocket, close to the two-fold axis. The X-ray structure of the E53Q, E56Q, E57Q, E60Q+R59M recombinant horse L-chain apoferritin has been obtained at a higher resolution (1.16A) than previously reported for any mammalian apoferritins. Similar evidence for a metal-free molecule derived from haemin was found in the electron density map of horse spleen apoferritin (at a resolution of 1.5A). The out-of-plane distortion of the observed porphyrin is clearly compatible with an N-alkyl porphyrin. We conclude that L-chain ferritins are capable of binding and demetallating haemin, generating in the process N-ethylprotoporphyrin IX both in vivo and in vitro.
Structural analysis of haemin demetallation by L-chain apoferritins.,de Val N, Declercq JP, Lim CK, Crichton RR J Inorg Biochem. 2012 Mar 9;112C:77-84. PMID:22561545[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ de Val N, Declercq JP, Lim CK, Crichton RR. Structural analysis of haemin demetallation by L-chain apoferritins. J Inorg Biochem. 2012 Mar 9;112C:77-84. PMID:22561545 doi:10.1016/j.jinorgbio.2012.02.031
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