ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Encapsulins in Terpene Biosynthesis: Enzyme Nanoreactors in Bacterial Secondary Metabolism.Biochemistry · 2026Review
- Directed evolution of multimeric proteins is enabled by dual-compensatory gene duplication.bioRxiv : the preprint server for biology · 2026Article
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance.ACS nano · 2024Article
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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.
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