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| | ==Crystal structure of Frog M-ferritin K104E mutant== | | ==Crystal structure of Frog M-ferritin K104E mutant== |
| - | <StructureSection load='5xhn' size='340' side='right' caption='[[5xhn]], [[Resolution|resolution]] 1.63Å' scene=''> | + | <StructureSection load='5xhn' size='340' side='right'caption='[[5xhn]], [[Resolution|resolution]] 1.63Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xhn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XHN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xhn]] 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=5XHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XHN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.63Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xhi|5xhi]], [[5xhm|5xhm]], [[5xho|5xho]]</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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5xhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhn OCA], [https://pdbe.org/5xhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xhn RCSB], [https://www.ebi.ac.uk/pdbsum/5xhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhn ProSAT]</span></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=5xhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhn OCA], [http://pdbe.org/5xhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xhn RCSB], [http://www.ebi.ac.uk/pdbsum/5xhn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5xhn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5xhn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Jagdev, M K]] | + | [[Category: Lithobates catesbeianus]] |
| - | [[Category: Vasudevan, D]] | + | [[Category: Jagdev MK]] |
| - | [[Category: Ferritin]] | + | [[Category: Vasudevan D]] |
| - | [[Category: M-ferritin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
Preparation of modified and hybrid ferritin provides a great opportunity to understand the mechanisms of iron loading/unloading, protein self-assembly, size constrained nanomaterial synthesis and targeted drug delivery. However, the large size (M.W.=490kDa) has been limiting the separation of different modified and/or hybrid ferritin nanocages from each other in their intact assembled form and further characterization. Native polyacrylamide gel electrophoresis (PAGE) separates proteins on the basis of both charge and mass, while maintaining their overall native structure and activity. Altering surface charge distribution by substitution of amino acid residues located at the external surface of ferritin (K104E & D40A) affected the migration rate in native PAGE while internal modification had little effect. Crystal structures confirmed that ferritin nanocages made up of subunits with single amino acid substitutions retain the overall structure of ferritin nanocage. Taking advantage of K104E migration behavior, formation of hybrid ferritins with subunits of wild type (WT) and K104E were confirmed and separated in native PAGE. Cage integrity and iron loading ability (ferritin activity) were also tested. The migration pattern of hybrid ferritins in native PAGE depends on the subunit ratio (WT: K104E) in the ferritin cage. Our work shows that native PAGE can be exploited in nanobiotechnology, by analyzing modifications of large proteins like ferritin. SIGNIFICANCE: Native PAGE, a simple, straight-forward technique, can be used to analyze small modification (by altering external surface charge) in large proteins like ferritin, without disintegrating its self-assembled nanocage structure. In doing so, native PAGE can complement the information obtained from mass spectrometry. The confirmation and separation of modified and hybrid ferritin protein nanocages in native PAGE, opens up various prospects of bio-conjugation, which can be useful in targeted drug delivery, nanobiotechnology and in understanding nature's idea of synthesizing hybrid ferritins in different human tissues.
Surface charge dependent separation of modified and hybrid ferritin in native PAGE: Impact of lysine 104.,Subhadarshanee B, Mohanty A, Jagdev MK, Vasudevan D, Behera RK Biochim Biophys Acta. 2017 Jul 21;1865(10):1267-1273. doi:, 10.1016/j.bbapap.2017.07.012. PMID:28739445[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Subhadarshanee B, Mohanty A, Jagdev MK, Vasudevan D, Behera RK. Surface charge dependent separation of modified and hybrid ferritin in native PAGE: Impact of lysine 104. Biochim Biophys Acta. 2017 Jul 21;1865(10):1267-1273. doi:, 10.1016/j.bbapap.2017.07.012. PMID:28739445 doi:http://dx.doi.org/10.1016/j.bbapap.2017.07.012
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