9DND
Pseudosymmetric protein nanocage GI4 -F7 (local refinement)
Summary for 9DND
| Entry DOI | 10.2210/pdb9dnd/pdb |
| EMDB information | 47036 |
| Descriptor | Pseudosymmetric protein nanocages GI4 A Chain, Pseudosymmetric protein nanocages GI4 C Chain, Pseudosymmetric protein nanocages GI4 B Chain (3 entities in total) |
| Functional Keywords | fusion protein, structural genomics, seattle structural genomics center for infectious disease, ssgcid, pseudosymmetric protein nanocages, viral protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 4 |
| Total formula weight | 94307.78 |
| Authors | Park, Y.J.,Dowling, Q.M.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),King, N.P.,Veesler, D. (deposition date: 2024-09-17, release date: 2024-12-18, Last modification date: 2025-02-26) |
| Primary citation | Dowling, Q.M.,Park, Y.J.,Fries, C.N.,Gerstenmaier, N.C.,Ols, S.,Yang, E.C.,Wargacki, A.J.,Dosey, A.,Hsia, Y.,Ravichandran, R.,Walkey, C.D.,Burrell, A.L.,Veesler, D.,Baker, D.,King, N.P. Hierarchical design of pseudosymmetric protein nanocages. Nature, 638:553-561, 2025 Cited by PubMed Abstract: Discrete protein assemblies ranging from hundreds of kilodaltons to hundreds of megadaltons in size are a ubiquitous feature of biological systems and perform highly specialized functions. Despite remarkable recent progress in accurately designing new self-assembling proteins, the size and complexity of these assemblies has been limited by a reliance on strict symmetry. Here, inspired by the pseudosymmetry observed in bacterial microcompartments and viral capsids, we developed a hierarchical computational method for designing large pseudosymmetric self-assembling protein nanomaterials. We computationally designed pseudosymmetric heterooligomeric components and used them to create discrete, cage-like protein assemblies with icosahedral symmetry containing 240, 540 and 960 subunits. At 49, 71 and 96 nm diameter, these nanocages are the largest bounded computationally designed protein assemblies generated to date. More broadly, by moving beyond strict symmetry, our work substantially broadens the variety of self-assembling protein architectures that are accessible through design. PubMed: 39695230DOI: 10.1038/s41586-024-08360-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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