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| ==Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid== | | ==Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid== |
| <StructureSection load='6b8f' size='340' side='right' caption='[[6b8f]], [[Resolution|resolution]] 1.06Å' scene=''> | | <StructureSection load='6b8f' size='340' side='right'caption='[[6b8f]], [[Resolution|resolution]] 1.06Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6b8f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B8F FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6b8f]] is a 1 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=6B8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B8F FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.06Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=6b8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b8f OCA], [https://pdbe.org/6b8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b8f RCSB], [https://www.ebi.ac.uk/pdbsum/6b8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b8f 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=6b8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b8f OCA], [http://pdbe.org/6b8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b8f RCSB], [http://www.ebi.ac.uk/pdbsum/6b8f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b8f 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;">
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| == Publication Abstract from PubMed ==
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| The formation of condensed matter typically involves a trade-off between structural order and flexibility. As the extent and directionality of interactions between atomic or molecular components increase, materials generally become more ordered but less compliant, and vice versa. Nevertheless, high levels of structural order and flexibility are not necessarily mutually exclusive; there are many biological (such as microtubules(1,2), flagella (3) , viruses(4,5)) and synthetic assemblies (for example, dynamic molecular crystals(6-9) and frameworks(10-13)) that can undergo considerable structural transformations without losing their crystalline order and that have remarkable mechanical properties(8,14,15) that are useful in diverse applications, such as selective sorption (16) , separation (17) , sensing (18) and mechanoactuation (19) . However, the extent of structural changes and the elasticity of such flexible crystals are constrained by the necessity to maintain a continuous network of bonding interactions between the constituents of the lattice. Consequently, even the most dynamic porous materials tend to be brittle and isolated as microcrystalline powders (14) , whereas flexible organic or inorganic molecular crystals cannot expand without fracturing. Owing to their rigidity, crystalline materials rarely display self-healing behaviour (20) . Here we report that macromolecular ferritin crystals with integrated hydrogel polymers can isotropically expand to 180 per cent of their original dimensions and more than 500 per cent of their original volume while retaining periodic order and faceted Wulff morphologies. Even after the separation of neighbouring ferritin molecules by 50 angstroms upon lattice expansion, specific molecular contacts between them can be reformed upon lattice contraction, resulting in the recovery of atomic-level periodicity and the highest-resolution ferritin structure reported so far. Dynamic bonding interactions between the hydrogel network and the ferritin molecules endow the crystals with the ability to resist fragmentation and self-heal efficiently, whereas the chemical tailorability of the ferritin molecules enables the creation of chemically and mechanically differentiated domains within single crystals.
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| Hyperexpandable, self-healing macromolecular crystals with integrated polymer networks.,Zhang L, Bailey JB, Subramanian RH, Tezcan FA Nature. 2018 May;557(7703):86-91. doi: 10.1038/s41586-018-0057-7. Epub 2018 May, 2. PMID:29720635<ref>PMID:29720635</ref>
| | ==See Also== |
| | | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6b8f" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Ferroxidase]] | | [[Category: Homo sapiens]] |
| [[Category: Human]] | | [[Category: Large Structures]] |
| [[Category: Bailey, J B]] | | [[Category: Bailey JB]] |
| [[Category: Subramanian, R]] | | [[Category: Subramanian R]] |
| [[Category: Tezcan, F A]] | | [[Category: Tezcan FA]] |
| [[Category: Zhang, L]] | | [[Category: Zhang L]] |
| [[Category: Hydrogel]]
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| [[Category: Oxidoreductase]]
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| [[Category: Polymer]]
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