4DYY
Crystal Structure of the Cu-adduct of Human H-Ferritin variant MIC1
Summary for 4DYY
| Entry DOI | 10.2210/pdb4dyy/pdb |
| Related | 2CEI 4DYX 4DYz 4DZ0 |
| Descriptor | Ferritin heavy chain, COPPER (II) ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | four-helix bundle, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 20502.23 |
| Authors | Tezcan, F.A.,Huard, D.J.E. (deposition date: 2012-02-29, release date: 2013-01-23, Last modification date: 2023-09-13) |
| Primary citation | Huard, D.J.,Kane, K.M.,Tezcan, F.A. Re-engineering protein interfaces yields copper-inducible ferritin cage assembly. Nat.Chem.Biol., 9:169-176, 2013 Cited by PubMed Abstract: The ability to chemically control protein-protein interactions would allow the interrogation of dynamic cellular processes and lead to a better understanding and exploitation of self-assembling protein architectures. Here we introduce a new engineering strategy--reverse metal-templated interface redesign (rMeTIR)--that transforms a natural protein-protein interface into one that only engages in selective response to a metal ion. We have applied rMeTIR to render the self-assembly of the cage-like protein ferritin controllable by divalent copper binding, which has allowed the study of the structure and stability of the isolated ferritin monomer, the demonstration of the primary role of conserved hydrogen-bonding interactions in providing geometric specificity for cage assembly and the uniform chemical modification of the cage interior under physiological conditions. Notably, copper acts as a structural template for ferritin assembly in a manner that is highly reminiscent of RNA sequences that template virus capsid formation. PubMed: 23340339DOI: 10.1038/nchembio.1163 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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