8R59
Structure of the Co(II) triggered TRAP (S33HK35H) protein cage (levo form)
This is a non-PDB format compatible entry.
Summary for 8R59
| Entry DOI | 10.2210/pdb8r59/pdb |
| EMDB information | 18904 |
| Descriptor | Transcription attenuation protein MtrB, COBALT (II) ION (2 entities in total) |
| Functional Keywords | trap protein, protein cage, virus like particle |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 264 |
| Total formula weight | 2202868.99 |
| Authors | Biela, A.P.,Heddle, J.G. (deposition date: 2023-11-16, release date: 2024-12-25, Last modification date: 2025-04-02) |
| Primary citation | Osinski, N.,Majsterkiewicz, K.,Pakosz-Stepien, Z.,Azuma, Y.,Biela, A.P.,Gawel, S.,Heddle, J.G. Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH-Dependent Assembly. Macromol Rapid Commun, 46:e2400712-e2400712, 2025 Cited by PubMed Abstract: The rational design and production of a novel series of engineered protein cages are presented, which have emerged as versatile and adaptable platforms with significant applications in biomedicine. These protein cages are assembled from multiple protein subunits, and precise control over their interactions is crucial for regulating assembly and disassembly, such as the on-demand release of encapsulated therapeutic agents. This approach employs a homo-undecameric, ring-shaped protein scaffold with strategically positioned metal binding sites. These engineered proteins can self-assemble into highly stable cages in the presence of cobalt or zinc ions. Furthermore, the cages can be disassembled on demand by employing external triggers such as chelating agents and changes in pH. Interestingly, for certain triggers, the disassembly process is reversible, allowing the cages to reassemble upon reversal or outcompeting of triggering conditions/agents. This work offers a promising platform for the development of advanced drug delivery systems and other biomedical applications. PubMed: 39676522DOI: 10.1002/marc.202400712 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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