5e1u
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of IrCp*-apo-Fr== | |
| + | <StructureSection load='5e1u' size='340' side='right' caption='[[5e1u]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5e1u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1U 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=IR3:IRIDIUM+(III)+ION'>IR3</scene>, <scene name='pdbligand=RIR:[(1,2,3,4,5-ETA)-1,2,3,4,5-PENTAMETHYLCYCLOPENTADIENYL]IRIDIUM(III)'>RIR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e2d|5e2d]]</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=5e1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1u OCA], [http://pdbe.org/5e1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1u RCSB], [http://www.ebi.ac.uk/pdbsum/5e1u PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5e1u" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Abe, S]] | [[Category: Abe, S]] | ||
| - | [[Category: Ueno, T]] | ||
[[Category: Fukumori, K]] | [[Category: Fukumori, K]] | ||
| + | [[Category: Maity, B]] | ||
| + | [[Category: Ueno, T]] | ||
| + | [[Category: Iron storage]] | ||
| + | [[Category: Metal binding protein]] | ||
Revision as of 18:42, 12 May 2016
Crystal structure of IrCp*-apo-Fr
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