5jac
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Sixty minutes iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A== | |
| + | <StructureSection load='5jac' size='340' side='right'caption='[[5jac]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jac]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JAC 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]] 1.18Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5jac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jac OCA], [https://pdbe.org/5jac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jac RCSB], [https://www.ebi.ac.uk/pdbsum/5jac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jac ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FRI2_LITCT FRI2_LITCT] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe2+ to Fe3+ at ferroxidase sites. By a combination of structural and spectroscopic techniques, Asp140, together with previously identified Glu57 and Glu136, is demonstrated to be an essential residue to promote the iron oxidation at the ferroxidase site. However, the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe2+ substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages. | ||
| - | + | Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity.,Bernacchioni C, Pozzi C, Di Pisa F, Mangani S, Turano P Chemistry. 2016 Sep 21. doi: 10.1002/chem.201602842. PMID:27650996<ref>PMID:27650996</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bernacchioni | + | <div class="pdbe-citations 5jac" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Mangani | + | ==See Also== |
| - | [[Category: | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| - | [[Category: Turano | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lithobates catesbeianus]] | ||
| + | [[Category: Bernacchioni C]] | ||
| + | [[Category: Di Pisa F]] | ||
| + | [[Category: Mangani S]] | ||
| + | [[Category: Pozzi C]] | ||
| + | [[Category: Turano P]] | ||
Current revision
Sixty minutes iron loaded Rana Catesbeiana H' ferritin variant E57A/E136A/D140A
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