ArticleJournal of structural biology2023
Structure and heterogeneity of a highly cargo-loaded encapsulin shell.
Article in Journal of structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Protein Nanocages as Versatile Vectors for Nucleic Acid Delivery: Main Systems and Their Loading Mechanisms.Molecular biotechnology · 2026Review
- Encapsulin-Protected Immunotherapeutic Complexes: Bacteria-Derived Nanoparticles for mRNA Delivery to Eukaryotic Cells.ChemMedChem · 2026Article
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- High-Fidelity In Vitro Packaging of Diverse Synthetic Cargo into Encapsulin Protein Cages.Angewandte Chemie (International ed. in English) · 2025Article
- Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Surface Engineering of the Encapsulin Nanocompartment ofACS omega · 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
- Structural Characterization ofMicroorganisms · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.Nature communications · 2024Article
- Heterologous Prime-Boost with Immunologically Orthogonal Protein Nanoparticles for Peptide Immunofocusing.ACS nano · 2024Article
- Encapsulation of Transketolase intoACS applied bio materials · 2024Article
- Article
- Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.bioRxiv : the preprint server for biology · 2024Article
- Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.Nature communications · 2024Article
- Heterologous Prime-Boost with Immunologically Orthogonal Protein Nanoparticles for Peptide Immunofocusing.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
- Update of
Authors and funding
3 authors.
Funding
Abstract
Encapsulins are self-assembling protein nanocompartments able to selectively encapsulate dedicated cargo enzymes. Encapsulins are widespread across bacterial and archaeal phyla and are involved in oxidative stress resistance, iron storage, and sulfur metabolism. Encapsulin shells exhibit icosahedral geometry and consist of 60, 180, or 240 identical protein subunits. Cargo encapsulation is mediated by the specific interaction of targeting peptides or domains, found in all cargo proteins, with the interior surface of the encapsulin shell during shell self-assembly. Here, we report the 2.53 Å cryo-EM structure of a heterologously produced and highly cargo-loaded T3 encapsulin shell from Myxococcus xanthus and explore the systems' structural heterogeneity. We find that exceedingly high cargo loading results in the formation of substantial amounts of distorted and aberrant shells, likely caused by a combination of unfavorable steric clashes of cargo proteins and shell conformational changes. Based on our cryo-EM structure, we determine and analyze the targeting peptide-shell binding mode. We find that both ionic and hydrophobic interactions mediate targeting peptide binding. Our results will guide future attempts at rationally engineering encapsulins for biomedical and biotechnological applications.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.