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[[Image:2cn7.gif|left|200px]]


{{Structure
==Recombinant human H ferritin, K86Q, E27D and E107D mutant==
|PDB= 2cn7 |SIZE=350|CAPTION= <scene name='initialview01'>2cn7</scene>, resolution 1.75&Aring;
<StructureSection load='2cn7' size='340' side='right'caption='[[2cn7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[2cn7]] is a 1 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=2CN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CN7 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cn7 OCA], [https://pdbe.org/2cn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2cn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cn7 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cn7 OCA], [http://www.ebi.ac.uk/pdbsum/2cn7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cn7 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/2cn7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cn7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ferritins are a family of proteins distributed widely in nature. In bacterial, plant, and animal cells, ferritin appears to serve as a soluble, bioavailable, and non-toxic form of iron provider. Ferritins from animal sources are heteropolymers composed of two types of subunit, H and L, which differ mainly by the presence (H) or absence (L) of active ferroxidase centres. We report the crystallographic structures of four human H apoferritin variants at a resolution of up to 1.5 Angstrom. Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The ferroxidase centre, which is composed of sites A and B, binds metal with a preference for the A site. In addition, distinct Zn(II)-binding sites were found in the 3-fold axes, 4-fold axes and on the cavity surface near the ferroxidase centre. To study the importance of the distance of the two metal atoms in the ferroxidase centre, single and double replacement of glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal binding and the correlation with Fe(II) oxidation rates are discussed.


'''RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT'''
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites.,Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541<ref>PMID:17070541</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cn7" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Ferritins are a family of proteins distributed widely in nature. In bacterial, plant, and animal cells, ferritin appears to serve as a soluble, bioavailable, and non-toxic form of iron provider. Ferritins from animal sources are heteropolymers composed of two types of subunit, H and L, which differ mainly by the presence (H) or absence (L) of active ferroxidase centres. We report the crystallographic structures of four human H apoferritin variants at a resolution of up to 1.5 Angstrom. Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The ferroxidase centre, which is composed of sites A and B, binds metal with a preference for the A site. In addition, distinct Zn(II)-binding sites were found in the 3-fold axes, 4-fold axes and on the cavity surface near the ferroxidase centre. To study the importance of the distance of the two metal atoms in the ferroxidase centre, single and double replacement of glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal binding and the correlation with Fe(II) oxidation rates are discussed.
*[[Ferritin 3D structures|Ferritin 3D structures]]
 
== References ==
==About this Structure==
<references/>
2CN7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CN7 OCA].
__TOC__
 
</StructureSection>
==Reference==
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17070541 17070541]
[[Category: Ferroxidase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Crichton, R R.]]
[[Category: Crichton RR]]
[[Category: Declercq, J P.]]
[[Category: Declercq JP]]
[[Category: Toussaint, L.]]
[[Category: Toussaint L]]
[[Category: apoferritin]]
[[Category: di-iron non-heme protein]]
[[Category: ferroxidase]]
[[Category: iron]]
[[Category: iron storage]]
[[Category: metal-binding]]
[[Category: oxidoreductase]]
[[Category: phosphorylation]]
 
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