9BJE
Encapsulin 1 of a two-component Family 2B encapsulin shell from Streptomyces lydicus
Summary for 9BJE
| Entry DOI | 10.2210/pdb9bje/pdb |
| EMDB information | 44632 |
| Descriptor | Crp/Fnr family transcriptional regulator (1 entity in total) |
| Functional Keywords | encapsulin, nanocompartment, virus like particle |
| Biological source | Streptomyces lydicus |
| Total number of polymer chains | 1 |
| Total formula weight | 52256.59 |
| Authors | Andreas, M.P.,Dutcher, C.,Giessen, T.W. (deposition date: 2024-04-25, release date: 2025-04-30, Last modification date: 2025-09-10) |
| Primary citation | Dutcher, C.A.,Andreas, M.P.,Giessen, T.W. A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling. Adv Sci, 12:e03617-e03617, 2025 Cited by PubMed Abstract: Protein shells or capsids are a widespread form of compartmentalization in nature. Viruses use protein capsids to protect and transport their genomes while many cellular organisms use protein shells for varied metabolic purposes. These protein-based compartments often exhibit icosahedral symmetry and consist of a small number of structural components with defined roles. Encapsulins are a prevalent protein-based compartmentalization strategy in prokaryotes. All encapsulins studied thus far consist of a single shell protein that adopts the viral Hong Kong 97 (HK97)-fold. Here, the characterization of a Family 2B two-component encapsulin from Streptomyces lydicus is reported. The differential assembly behavior of the two shell components and their ability to co-assemble into mixed shells with variable shell composition is demonstrated. The structures of both shell proteins are determined using cryo-electron microscopy. Using 3D-classification and cross-linking studies, the irregular tiling of mixed shells is highlighted. This work expands the known assembly modes of HK97-fold proteins and lays the foundation for future functional and engineering studies on two-component encapsulins. PubMed: 40557621DOI: 10.1002/advs.202503617 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.58 Å) |
Structure validation
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