7JGK
Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 100K
Summary for 7JGK
| Entry DOI | 10.2210/pdb7jgk/pdb |
| Related | 5CMR 5UP7 5UP8 5UP9 |
| Descriptor | Ferritin heavy chain, N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide, NICKEL (II) ION, ... (5 entities in total) |
| Functional Keywords | protein-mof, ferritin-mof, self-assembly, ferritin, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21507.48 |
| Authors | Bailey, J.B.,Tezcan, F.A. (deposition date: 2020-07-19, release date: 2020-10-14, Last modification date: 2023-10-18) |
| Primary citation | Bailey, J.B.,Tezcan, F.A. Tunable and Cooperative Thermomechanical Properties of Protein-Metal-Organic Frameworks. J.Am.Chem.Soc., 142:17265-17270, 2020 Cited by PubMed Abstract: 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 °C and a hysteresis window of ∼10 °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. PubMed: 32972136DOI: 10.1021/jacs.0c07835 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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