View source for 5e2d


==Crystal structure of IrCp*/Pd(allyl)-apo-Fr==
<StructureSection load='5e2d' size='340' side='right'caption='[[5e2d]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5e2d]] 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=5E2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E2D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</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=IR:IRIDIUM+ION'>IR</scene>, <scene name='pdbligand=IR3:IRIDIUM+(III)+ION'>IR3</scene>, <scene name='pdbligand=PD:PALLADIUM+ION'>PD</scene>, <scene name='pdbligand=PLL:PALLADIUM(II)+ALLYL+COMPLEX'>PLL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5e2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e2d OCA], [https://pdbe.org/5e2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e2d RCSB], [https://www.ebi.ac.uk/pdbsum/5e2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e2d ProSAT]</span></td></tr>
</table>
== 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Natural protein-based microcompartments containing multiple enzymes promote cascade reactions within cells. We use the apo-ferritin protein cage to mimic such biocompartments by immobilizing two organometallic Ir and Pd complexes into the single protein cage. Precise locations of the metals and their accumulation mechanism were studied by X-ray crystallography.

Immobilization of two organometallic complexes into a single cage to construct protein-based microcompartments.,Maity B, Fukumori K, Abe S, Ueno T Chem Commun (Camb). 2016 Apr 7;52(31):5463-6. doi: 10.1039/c6cc00679e. PMID:27021005<ref>PMID:27021005</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e2d" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Abe S]]
[[Category: Fukumori K]]
[[Category: Maity B]]
[[Category: Ueno T]]