3wvu

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Current revision (08:47, 20 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wvu]] 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=3WVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WVU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wvu]] 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=3WVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WVU FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wvv|3wvv]], [[3wvw|3wvw]]</div></td></tr>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvu OCA], [https://pdbe.org/3wvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wvu RCSB], [https://www.ebi.ac.uk/pdbsum/3wvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wvu 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=3wvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvu OCA], [https://pdbe.org/3wvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wvu RCSB], [https://www.ebi.ac.uk/pdbsum/3wvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wvu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3wvu" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abe, S]]
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[[Category: Abe S]]
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[[Category: Fujita, K]]
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[[Category: Fujita K]]
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[[Category: Hikage, T]]
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[[Category: Hikage T]]
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[[Category: Kizaka-Kondoh, S]]
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[[Category: Kizaka-Kondoh S]]
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[[Category: Kuchimaru, T]]
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[[Category: Kuchimaru T]]
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[[Category: Tanaka, Y]]
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[[Category: Tanaka Y]]
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[[Category: Ueno, T]]
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[[Category: Ueno T]]
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[[Category: Metal binding protein]]
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[[Category: PSI, Protein structure initiative]]
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Current revision

Crystal Structure of RuCO/apo-R52CFr

PDB ID 3wvu

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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