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==Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 278K== | ==Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 278K== | ||
<StructureSection load='7jgo' size='340' side='right'caption='[[7jgo]]' scene=''> | <StructureSection load='7jgo' size='340' side='right'caption='[[7jgo]], [[Resolution|resolution]] 3.08Å' 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=7JGO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JGO FirstGlance]. <br> | <table><tr><td colspan='2'>[[7jgo]] 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=7JGO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JGO FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jgo OCA], [http://pdbe.org/7jgo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jgo RCSB], [http://www.ebi.ac.uk/pdbsum/7jgo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jgo ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=V9Y:N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide'>V9Y</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5up7|5up7]], [[5up8|5up8]], [[5up9|5up9]], [[5cmr|5cmr]]</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='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'>[http://proteopedia.org/fgij/fg.htm?mol=7jgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jgo OCA], [http://pdbe.org/7jgo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jgo RCSB], [http://www.ebi.ac.uk/pdbsum/7jgo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jgo ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== 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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We recently introduced protein-metal-organic frameworks (protein-MOFs) as chemically designed protein crystals, composed of ferritin nodes that predictably assemble into 3D lattices upon coordination of various metal ions and ditopic, hydroxamate-based linkers. Owing to their unique tripartite construction, protein-MOFs possess extremely sparse lattice connectivity, suggesting that they might display unusual thermomechanical properties. Leveraging the synthetic modularity of ferritin-MOFs, we investigated the temperature-dependent structural dynamics of six distinct frameworks. Our results show that the thermostabilities of ferritin-MOFs can be tuned through the metal component or the presence of crowding agents. Our studies also reveal a framework that undergoes a reversible and isotropic first-order phase transition near-room temperature, corresponding to a 4% volumetric change within 1 degrees C and a hysteresis window of approximately 10 degrees C. This highly cooperative crystal-to-crystal transformation, which stems from the soft crystallinity of ferritin-MOFs, illustrates the advantage of modular construction strategies in discovering tunable-and unpredictable-material properties. | |||
Tunable and Cooperative Thermomechanical Properties of Protein-Metal-Organic Frameworks.,Bailey JB, Tezcan FA J Am Chem Soc. 2020 Oct 5. doi: 10.1021/jacs.0c07835. PMID:32972136<ref>PMID:32972136</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7jgo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ferroxidase]] | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bailey | [[Category: Bailey, J B]] | ||
[[Category: Tezcan | [[Category: Tezcan, F A]] | ||
[[Category: Ferritin]] | |||
[[Category: Ferritin-mof]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Protein-mof]] | |||
[[Category: Self-assembly]] |