5UP7
Crystal Structure of the Ni-bound Human Heavy-Chain Ferritin 122H-delta C-star variant
Summary for 5UP7
| Entry DOI | 10.2210/pdb5up7/pdb |
| Related | 5CMQ 5CMR 5UP8 5UP9 |
| Descriptor | Ferritin heavy chain, NICKEL (II) ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, node, maxi-ferritin |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21593.43 |
| Authors | Bailey, J.B.,Zhang, L.,Chiong, J.A.,Ahn, S.,Tezcan, F.A. (deposition date: 2017-02-01, release date: 2017-06-21, Last modification date: 2023-10-04) |
| Primary citation | Bailey, J.B.,Zhang, L.,Chiong, J.A.,Ahn, S.,Tezcan, F.A. Synthetic Modularity of Protein-Metal-Organic Frameworks. J. Am. Chem. Soc., 139:8160-8166, 2017 Cited by PubMed Abstract: Previously, we adopted the construction principles of metal-organic frameworks (MOFs) to design a 3D crystalline protein lattice in which pseudospherical ferritin nodes decorated on their C symmetric vertices with Zn coordination sites were connected via a ditopic benzene-dihydroxamate linker. In this work, we have systematically varied both the metal ions presented at the vertices of the ferritin nodes (Zn(II), Ni(II), and Co(II)) and the synthetic dihydroxamate linkers, which yielded an expanded library of 15 ferritin-MOFs with the expected body-centered (cubic or tetragonal) lattice arrangements. Crystallographic and small-angle X-ray scattering (SAXS) analyses indicate that lattice symmetries and dimensions of ferritin-MOFs can be dictated by both the metal and linker components. SAXS measurements on bulk crystalline samples reveal that some ferritin-MOFs can adopt multiple lattice conformations, suggesting dynamic behavior. This work establishes that the self-assembly of ferritin-MOFs is highly robust and that the synthetic modularity that underlies the structural diversity of conventional MOFs can also be applied to the self-assembly of protein-based crystalline materials. PubMed: 28590729DOI: 10.1021/jacs.7b01202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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