ArticleScientific reports2021
The encapsulin from Thermotoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 37 citations in OpenAlex.
- Review
- Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane.Science advances · 2026Article
- Protein nanocages: A new frontier in mucosal vaccine delivery and immune activation.Human vaccines & immunotherapeutics · 2025Review
- Encapsulins: catalysis inside a shell.Current opinion in microbiology · 2025Review
- Assembly of Matryoshka-Type Protein Nanocages for Compartmentalized Oxygen Sensing.Nano letters · 2025Article
- In situ and in vitro cryo-EM reveal structures of mycobacterial encapsulin assembly intermediates.Communications biology · 2025Article
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024Review
- Structural Characterization ofMicroorganisms · 2024Article
- Article
- Encapsulation of Transketolase intoACS applied bio materials · 2024Article
- Encapsulated Ferritin-like Proteins: A Structural Perspective.Biomolecules · 2024Review
- Article
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- A widespread bacterial protein compartment sequesters and stores elemental sulfur.Science advances · 2024Article
- Structure and heterogeneity of a highly cargo-loaded encapsulin shell.Journal of structural biology · 2023Article
- Structure and heterogeneity of a highly cargo-loaded encapsulin shell.bioRxiv : the preprint server for biology · 2023Article
- Charge Transport across Proteins inside Proteins: Tunneling across Encapsulin Protein Cages and the Effect of Cargo Proteins.Biomolecules · 2023Article
- Encapsulins: Structure, Properties, and Biotechnological Applications.Biochemistry. Biokhimiia · 2023Review
- Encapsulins.Annual review of biochemistry · 2022Review
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based 'organelles' found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~ 25-50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure-function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model Thermotoga maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryo-EM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the Thermotoga maritima encapsulin, the decameric cargo protein with fivefold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier-it also plays a significant role in the structure and function of the cargo enzyme.
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