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-Structure paper
Title | A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling. |
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Journal, issue, pages | Adv Sci (Weinh), Page e03617, Year 2025 |
Publish date | Jun 25, 2025 |
![]() | Cassandra A Dutcher / Michael P Andreas / Tobias W Giessen / ![]() |
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 ...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. |
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Methods | EM (single particle) |
Resolution | 2.58 - 2.59 Å |
Structure data | EMDB-44603, PDB-9bix: EMDB-44632, PDB-9bje: |
Source |
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![]() | VIRUS LIKE PARTICLE / encapsulin / nanocompartment |