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| | <StructureSection load='6ipc' size='340' side='right'caption='[[6ipc]], [[Resolution|resolution]] 4.44Å' scene=''> | | <StructureSection load='6ipc' size='340' side='right'caption='[[6ipc]], [[Resolution|resolution]] 4.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ipc]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ipc]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IPC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 4.443Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=6ipc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ipc OCA], [http://pdbe.org/6ipc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ipc RCSB], [http://www.ebi.ac.uk/pdbsum/6ipc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ipc ProSAT]</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=6ipc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ipc OCA], [https://pdbe.org/6ipc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ipc RCSB], [https://www.ebi.ac.uk/pdbsum/6ipc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ipc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN]] 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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). | + | [https://www.uniprot.org/uniprot/FRIH_HUMAN FRIH_HUMAN] 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. 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ipc" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ipc" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferroxidase]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, H]] | + | [[Category: Chen H]] |
| - | [[Category: Zang, J C]] | + | [[Category: Zang JC]] |
| - | [[Category: Zhao, G]] | + | [[Category: Zhao G]] |
| - | [[Category: 8-mer]]
| + | |
| - | [[Category: Ferritin]]
| + | |
| - | [[Category: Inner disulfide bond]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
FRIH_HUMAN 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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
Publication Abstract from PubMed
Constructing different protein nanostructures with high-order discrete architectures by using one single building block remains a challenge. Here, we present a simple, effective disulfide-mediated approach to prepare a set of protein nanocages with different geometries from single building block. By genetically deleting an inherent intra-subunit disulfide bond, we can render the conversion of an 8-mer bowl-like protein architecture (NF-8) into a 24-mer ferritin-like nanocage in solution, while selective insertion of an inter-subunit disulfide bond into NF-8 triggers its conversion into a 16-mer lenticular nanocage. Deletion of the same intra-subunit disulfide bond and insertion of the inter-subunit disulfide bond results in the conversion of NF-8 into a 48-mer protein nanocage in solution. Thus, in the laboratory, simple mutation of one protein building block can generate three different protein nanocages in a manner that is highly reminiscent of natural pentamer building block originating from viral capsids that self-assemble into protein assemblies with different symmetries.
Disulfide-mediated conversion of 8-mer bowl-like protein architecture into three different nanocages.,Zang J, Chen H, Zhang X, Zhang C, Guo J, Du M, Zhao G Nat Commun. 2019 Feb 15;10(1):778. doi: 10.1038/s41467-019-08788-9. PMID:30770832[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zang J, Chen H, Zhang X, Zhang C, Guo J, Du M, Zhao G. Disulfide-mediated conversion of 8-mer bowl-like protein architecture into three different nanocages. Nat Commun. 2019 Feb 15;10(1):778. doi: 10.1038/s41467-019-08788-9. PMID:30770832 doi:http://dx.doi.org/10.1038/s41467-019-08788-9
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