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7o65

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Current revision

Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 90 minutes showing either a dioxygen or a superoxide anion coordinated to iron ions in the ferroxidase site

Structural highlights

7o65 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J. A human mitochondrial ferritin encoded by an intronless gene. J Biol Chem. 2001 Jul 6;276(27):24437-40. Epub 2001 Apr 25. PMID:11323407 doi:http://dx.doi.org/10.1074/jbc.C100141200
↑ Langlois d'Estaintot B, Santambrogio P, Granier T, Gallois B, Chevalier JM, Precigoux G, Levi S, Arosio P. Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala. J Mol Biol. 2004 Jul 2;340(2):277-93. PMID:15201052 doi:10.1016/j.jmb.2004.04.036
↑ Ciambellotti S, Pratesi A, Tassone G, Turano P, Mangani S, Pozzi C. Iron Binding in the Ferroxidase Site of Human Mitochondrial Ferritin. Chemistry. 2021 Aug 3. doi: 10.1002/chem.202102270. PMID:34343376 doi:http://dx.doi.org/10.1002/chem.202102270

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7o65"

@@ Line 3: / Line 3: @@
 <StructureSection load='7o65' size='340' side='right'caption='[[7o65]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7o65]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O65 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7o65]] 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=7O65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O65 FirstGlance]. <br>
-</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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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]] 1.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7o63|7o63]], [[7o64|7o64]]</div></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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=7o65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o65 OCA], [https://pdbe.org/7o65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o65 RCSB], [https://www.ebi.ac.uk/pdbsum/7o65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o65 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>
+[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 ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 7o65" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ferritin 3D structures|Ferritin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ferroxidase]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ciambellotti, S]]
+[[Category: Ciambellotti S]]
-[[Category: Mangani, S]]
+[[Category: Mangani S]]
-[[Category: Pozzi, C]]
+[[Category: Pozzi C]]
-[[Category: Tassone, G]]
+[[Category: Tassone G]]
-[[Category: Turano, P]]
+[[Category: Turano P]]
-[[Category: Dioxygen]]
-[[Category: Ferroxidase site]]
-[[Category: Hmtf]]
-[[Category: Human mitochondrial ferritin]]
-[[Category: Oxidoreductase]]
-[[Category: Superoxide anion]]
-[[Category: Time-controlled iron loading]]

7o65

From Proteopedia

Current revision

Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 90 minutes showing either a dioxygen or a superoxide anion coordinated to iron ions in the ferroxidase site

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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