3o7r: Difference between revisions

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==Crystal structure of Ru(p-cymene)/apo-H49AFr==
==Crystal structure of Ru(p-cymene)/apo-H49AFr==
<StructureSection load='3o7r' size='340' side='right' caption='[[3o7r]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3o7r' size='340' side='right'caption='[[3o7r]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o7r]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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"><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">[[3o7s|3o7s]]</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 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7r RCSB], [http://www.ebi.ac.uk/pdbsum/3o7r PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[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).
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>


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

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