7w7j

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (17:37, 29 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of IrCp* immobilized apo-R52H-rHLFr (25 equiv)==
==Crystal structure of IrCp* immobilized apo-R52H-rHLFr (25 equiv)==
-
<StructureSection load='7w7j' size='340' side='right'caption='[[7w7j]]' scene=''>
+
<StructureSection load='7w7j' size='340' side='right'caption='[[7w7j]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W7J FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7w7j]] 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=7W7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W7J FirstGlance]. <br>
-
</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=7w7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w7j OCA], [https://pdbe.org/7w7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w7j RCSB], [https://www.ebi.ac.uk/pdbsum/7w7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w7j ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#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=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=7w7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w7j OCA], [https://pdbe.org/7w7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w7j RCSB], [https://www.ebi.ac.uk/pdbsum/7w7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w7j ProSAT]</span></td></tr>
</table>
</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 7w7j" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abe S]]
[[Category: Abe S]]

Current revision

Crystal structure of IrCp* immobilized apo-R52H-rHLFr (25 equiv)

PDB ID 7w7j

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools