View source for 3wvw


==Crystal structure of RuCO/apo-WTFr==
<StructureSection load='3wvw' size='340' side='right'caption='[[3wvw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wvw]] 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=3WVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WVW 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]] 2&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene>, <scene name='pdbligand=RU1:BIS(OXIDANIUMYLIDYNEMETHYL)RUTHENIUM(2+)'>RU1</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=3wvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvw OCA], [https://pdbe.org/3wvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wvw RCSB], [https://www.ebi.ac.uk/pdbsum/3wvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wvw 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 ==
Protein cages have been utilized as templates in the development of biomaterials. Here we report protein engineering of the ferritin (Fr) cage for encapsulating carbon monoxide releasing molecules (CORMs) and release of CO gas which serves as a cell signaling molecule. The protein cages enable us to increase the half-life for CO release, providing a release rate that is 18-fold slower than the rate of a typical CORM, Ru(CO)3Cl(glycinate) (CORM-3). Moreover, the uptake ratio of the composite is about 4-fold greater than that of CORM-3. We found that these effects enhance the activation of nuclear factor kappaB 10-fold higher than CORM-3. The protein cage of Fr thus provides the basis for new CORMs that can be used for in vitro cell research.

Intracellular CO release from composite of ferritin and ruthenium carbonyl complexes.,Fujita K, Tanaka Y, Sho T, Ozeki S, Abe S, Hikage T, Kuchimaru T, Kizaka-Kondoh S, Ueno T J Am Chem Soc. 2014 Dec 3;136(48):16902-8. doi: 10.1021/ja508938f. Epub 2014 Nov , 19. PMID:25352251<ref>PMID:25352251</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wvw" 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: Fujita K]]
[[Category: Hikage T]]
[[Category: Kizaka-Kondoh S]]
[[Category: Kuchimaru T]]
[[Category: Tanaka Y]]
[[Category: Ueno T]]