View source for 7o63


==High resolution crystal structure of human mitochondrial ferritin (hMTF)==
<StructureSection load='7o63' size='340' side='right'caption='[[7o63]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7o63]] 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=7O63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O63 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7o63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o63 OCA], [https://pdbe.org/7o63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o63 RCSB], [https://www.ebi.ac.uk/pdbsum/7o63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o63 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FTMT_HUMAN FTMT_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.<ref>PMID:11323407</ref> <ref>PMID:15201052</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ferritins are nanocage proteins that store iron ions in their central cavity as hydrated ferric oxide biominerals. In mammals, further the L (light) and H (heavy) chains constituting cytoplasmic maxi-ferritins, an additional type of ferritin has been identified, the mitochondrial ferritin (MTF). Human MTF (hMTF) is a functional homopolymeric H-like ferritin performing the ferroxidase activity in its ferroxidase site (FS), in which Fe(II) is oxidized to Fe(III) in the presence of dioxygen. To better investigate its ferroxidase properties, here we performed time-lapse X-ray crystallography analysis of hMTF, providing structural evidence of how iron ions interact with hMTF and of their binding to the FS. Transient iron binding sites, populating the pathway along the cage from the iron entry channel to the catalytic center, were also identified. Furthermore, our kinetic data at variable iron loads indicate that the catalytic iron oxidation reaction occurs via a diferric peroxo intermediate followed by the formation of ferric-oxo species, with significant differences with respect to human H-type ferritin.

Iron Binding in the Ferroxidase Site of Human Mitochondrial Ferritin.,Ciambellotti S, Pratesi A, Tassone G, Turano P, Mangani S, Pozzi C Chemistry. 2021 Aug 3. doi: 10.1002/chem.202102270. PMID:34343376<ref>PMID:34343376</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7o63" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ciambellotti S]]
[[Category: Mangani S]]
[[Category: Pozzi C]]
[[Category: Tassone G]]
[[Category: Turano P]]