7o6d: Difference between revisions
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==Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 3 minutes under anaerobic environment== | ==Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 3 minutes under anaerobic environment== | ||
<StructureSection load='7o6d' size='340' side='right'caption='[[7o6d]]' scene=''> | <StructureSection load='7o6d' size='340' side='right'caption='[[7o6d]], [[Resolution|resolution]] 1.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6D FirstGlance]. <br> | <table><tr><td colspan='2'>[[7o6d]] 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=7O6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6D FirstGlance]. <br> | ||
</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=7o6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6d OCA], [https://pdbe.org/7o6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6d RCSB], [https://www.ebi.ac.uk/pdbsum/7o6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6d ProSAT]</span></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]] 1.47Å</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=FE2:FE+(II)+ION'>FE2</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=7o6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6d OCA], [https://pdbe.org/7o6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6d RCSB], [https://www.ebi.ac.uk/pdbsum/7o6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6d ProSAT]</span></td></tr> | |||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7o6d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ciambellotti S]] | [[Category: Ciambellotti S]] | ||
Latest revision as of 15:45, 1 February 2024
Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 3 minutes under anaerobic environmentCrystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 3 minutes under anaerobic environment
Structural highlights
FunctionFTMT_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.[1] [2] Publication Abstract from PubMedFerritins 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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