View source for 7emm


==Crystal structure of IrCp* immobilized apo-R52H-rHLFr==
<StructureSection load='7emm' size='340' side='right'caption='[[7emm]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7emm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EMM FirstGlance]. <br>
</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IR:IRIDIUM+ION'>IR</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=7emm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7emm OCA], [https://pdbe.org/7emm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7emm RCSB], [https://www.ebi.ac.uk/pdbsum/7emm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7emm 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 ==
The effect of the mutation at the core of the ferritin nanocage (apo-rHLFr) on the uptake of IrCp* has been investigated by structural and spectroscopic methods. Site-specific mutations of two polar residues viz., Asp38 and Arg52 were investigated. The uptake of IrCp* was increased by about 1.5-fold on mutation of Arg52 by His compared to the wild-type variant, while mutation of Asp38 by His had no effect on the uptake. All the variants of the Ir-embedded ferritin cages remained as stable as the wild-type analogue. These hybrid bio-nanocages of ferritin were found to efficiently catalyze transfer hydrogenation of various substituted acetophenones forming the corresponding chiral alcohols with up to 88 % conversion and 70 % enantioselectivity. An electron-withdrawing substituent on the reactant enhanced the Turnover frequency of the reaction. Molecular docking analyses suggested that the substrate binds in different orientations at the active site in different mutants of the nanocage.

Controlled Uptake of an Iridium Complex inside Engineered apo-Ferritin Nanocages: Study of Structure and Catalysis.,Taher M, Maity B, Nakane T, Abe S, Ueno T, Mazumdar S Angew Chem Int Ed Engl. 2022 Jan 10:e202116623. doi: 10.1002/anie.202116623. PMID:35005820<ref>PMID:35005820</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7emm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Abe, S]]
[[Category: Maity, B]]
[[Category: Mazumdar, S]]
[[Category: Nakane, T]]
[[Category: Taher, M]]
[[Category: Ueno, T]]
[[Category: Ir binding]]
[[Category: Iron storage protein]]
[[Category: Metal binding protein]]