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| | <StructureSection load='2za6' size='340' side='right'caption='[[2za6]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='2za6' size='340' side='right'caption='[[2za6]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2za6]] 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=2ZA6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZA6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2za6]] 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=2ZA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZA6 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></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]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za7|2za7]], [[2za8|2za8]]</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za6 OCA], [http://pdbe.org/2za6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za6 RCSB], [http://www.ebi.ac.uk/pdbsum/2za6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2za6 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=2za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za6 OCA], [https://pdbe.org/2za6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2za6 RCSB], [https://www.ebi.ac.uk/pdbsum/2za6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2za6 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). |
| | == 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: Heddle, J G]] | + | [[Category: Heddle JG]] |
| - | [[Category: Mishima, Y]] | + | [[Category: Mishima Y]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park S-Y]] |
| - | [[Category: Tame, J R.H]] | + | [[Category: Tame JRH]] |
| - | [[Category: Yamashita, I]] | + | [[Category: Yamashita I]] |
| - | [[Category: Acetylation]]
| + | |
| - | [[Category: Ferric iron binding]]
| + | |
| - | [[Category: Iron storage]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| 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
The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of 24 L-chain subunits, in acidic solution was studied. Using two rLF mutants, lacking four (Fer4) or eight (Fer8) N-terminal amino acid residues, the effect of N-terminal residues on the protein's stability was investigated. Of the two mutants and wild-type rLF, the tertiary and secondary structures of Fer8 were found to be most sensitive to an acidic environment. The Fer8 protein dissociated easily into subunit dimers at or below pH 2.0. Comparing the crystal structures of the mutant proteins, deletion of the N-terminal residues was found to result in fewer inter- and intra-subunit hydrogen bonds. The loss of these bonds is assumed to be responsible for lower endurance against acidic denaturation in N-terminus-deleted mutants. These results indicated that the inter- and intra-subunit hydrogen bonds of N-terminal residues affect the denaturation, especially oligomer formation of apoferritin subunits and will be of use in designing ferritin-based nanodevices.
Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment.,Yoshizawa K, Mishima Y, Park SY, Heddle JG, Tame JR, Iwahori K, Kobayashi M, Yamashita I J Biochem. 2007 Dec;142(6):707-13. Epub 2007 Oct 15. PMID:17938140[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yoshizawa K, Mishima Y, Park SY, Heddle JG, Tame JR, Iwahori K, Kobayashi M, Yamashita I. Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment. J Biochem. 2007 Dec;142(6):707-13. Epub 2007 Oct 15. PMID:17938140 doi:10.1093/jb/mvm187
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