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| | ==Horse L type ferritin iron loaded for 60 minutes== | | ==Horse L type ferritin iron loaded for 60 minutes== |
| - | <StructureSection load='5lg2' size='340' side='right' caption='[[5lg2]], [[Resolution|resolution]] 2.22Å' scene=''> | + | <StructureSection load='5lg2' size='340' side='right'caption='[[5lg2]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lg2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LG2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lg2]] 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=5LG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LG2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</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]] 2.22Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=5lg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg2 OCA], [https://pdbe.org/5lg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lg2 RCSB], [https://www.ebi.ac.uk/pdbsum/5lg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg2 ProSAT]</span></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=5lg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg2 OCA], [http://pdbe.org/5lg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lg2 RCSB], [http://www.ebi.ac.uk/pdbsum/5lg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5lg2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5lg2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| - | [[Category: Mangani, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Pisa, F Di]] | + | [[Category: Di Pisa F]] |
| - | [[Category: Pozzi, C]] | + | [[Category: Mangani S]] |
| - | [[Category: Ferritin]] | + | [[Category: Pozzi C]] |
| - | [[Category: Iron]]
| + | |
| - | [[Category: L-type]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Mineralization]]
| + | |
| Structural highlights
5lg2 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.22Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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).
Publication Abstract from PubMed
X-ray structures of homopolymeric L-ferritin obtained by freezing protein crystals at increasing exposure times to a ferrous solution showed the progressive formation of a triiron cluster on the inner cage surface of each subunit. After 60 min exposure, a fully assembled (mu3-oxo)Tris[(mu2-peroxo)(mu2-glutamato-kappaO:kappaO')](glutamato-kappaO)(diaqu o)triiron(III) anionic cluster appears in human L-ferritin. Glu60, Glu61, and Glu64 provide the anchoring of the cluster to the protein cage. Glu57 shuttles incoming iron ions toward the cluster. We observed a similar metallocluster in horse spleen L-ferritin, indicating that it represents a common feature of mammalian L-ferritins. The structures suggest a mechanism for iron mineral formation at the protein interface. The functional significance of the observed patch of carboxylate side chains and resulting metallocluster for biomineralization emerges from the lower iron oxidation rate measured in the E60AE61AE64A variant of human L-ferritin, leading to the proposal that the observed metallocluster corresponds to the suggested, but yet unobserved, nucleation site of L-ferritin.
Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (mu3-oxo)Tris[(mu2-peroxo)] triiron(III) cluster.,Pozzi C, Ciambellotti S, Bernacchioni C, Di Pisa F, Mangani S, Turano P Proc Natl Acad Sci U S A. 2017 Feb 15. pii: 201614302. doi:, 10.1073/pnas.1614302114. PMID:28202724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pozzi C, Ciambellotti S, Bernacchioni C, Di Pisa F, Mangani S, Turano P. Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (mu3-oxo)Tris[(mu2-peroxo)] triiron(III) cluster. Proc Natl Acad Sci U S A. 2017 Feb 15. pii: 201614302. doi:, 10.1073/pnas.1614302114. PMID:28202724 doi:http://dx.doi.org/10.1073/pnas.1614302114
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