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3o7r: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#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;'>[[3o7s|3o7s]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=3o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7r OCA], [https://pdbe.org/3o7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7r RCSB], [https://www.ebi.ac.uk/pdbsum/3o7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7r ProSAT]</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=3o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7r OCA], [https://pdbe.org/3o7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7r RCSB], [https://www.ebi.ac.uk/pdbsum/3o7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. 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).  
[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spherical protein cages such as an iron storage protein, ferritin, have great potential as nanometer-scale capsules to assemble and store metal ions and complexes. We report herein the synthesis of a composite of an apo-ferritin cage and Ru(p-cymene) complexes. Ru complexes were efficiently incorporated into the ferritin cavity without degradation of its cage structure. X-Ray crystallography revealed that the Ru complexes were immobilized on the interior surface of the cage mainly by the coordination of histidine residues.
 
Incorporation of organometallic Ru complexes into apo-ferritin cage.,Takezawa Y, Bockmann P, Sugi N, Wang Z, Abe S, Murakami T, Hikage T, Erker G, Watanabe Y, Kitagawa S, Ueno T Dalton Trans. 2011 Mar 14;40(10):2190-5. Epub 2010 Nov 26. PMID:21113534<ref>PMID:21113534</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3o7r" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abe, S]]
[[Category: Abe S]]
[[Category: Bockmann, P]]
[[Category: Bockmann P]]
[[Category: Erker, G]]
[[Category: Erker G]]
[[Category: Hikage, T]]
[[Category: Hikage T]]
[[Category: Kitagawa, S]]
[[Category: Kitagawa S]]
[[Category: Murakami, T]]
[[Category: Murakami T]]
[[Category: Sugi, N]]
[[Category: Sugi N]]
[[Category: Takezawa, Y]]
[[Category: Takezawa Y]]
[[Category: Ueno, T]]
[[Category: Ueno T]]
[[Category: Wang, Z]]
[[Category: Wang Z]]
[[Category: Watanabe, Y]]
[[Category: Watanabe Y]]
[[Category: Artificial metalloprotein]]
[[Category: Iron storage protein]]
[[Category: Light chain apoferritin]]
[[Category: Metal binding protein]]

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