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==Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 1 minute.== | ==Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 1 minute.== | ||
<StructureSection load='7o64' size='340' side='right'caption='[[7o64]]' scene=''> | <StructureSection load='7o64' size='340' side='right'caption='[[7o64]], [[Resolution|resolution]] 1.96Å' 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=7O64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O64 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7o64]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O64 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=7o64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o64 OCA], [https://pdbe.org/7o64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o64 RCSB], [https://www.ebi.ac.uk/pdbsum/7o64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o64 ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7o63|7o63]]</div></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=7o64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o64 OCA], [https://pdbe.org/7o64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o64 RCSB], [https://www.ebi.ac.uk/pdbsum/7o64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o64 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 7o64" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ferroxidase]] | |||
[[Category: Large Structures]] | [[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: Ferroxidase site]] | |||
[[Category: Hmtf]] | |||
[[Category: Human mitochondrial ferritin]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Time-controlled iron loading]] | |||
Revision as of 19:00, 3 November 2021
Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 1 minute.Crystal structure of human mitochondrial ferritin (hMTF) Fe(II)-loaded for 1 minute.
Structural highlights
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 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. References
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