ArticleNature communications2024
Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Untapped enzymatic potential: dehalogenase- and peroxidase-driven PVC degradation by gene carriers in Tibetan plateau pikas.Microbiome · 2026Article
- Protein Nanocages as Versatile Vectors for Nucleic Acid Delivery: Main Systems and Their Loading Mechanisms.Molecular biotechnology · 2026Review
- Encapsulins in Terpene Biosynthesis: Enzyme Nanoreactors in Bacterial Secondary Metabolism.Biochemistry · 2026Review
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Encapsulins: catalysis inside a shell.Current opinion in microbiology · 2025Review
- Structural and Biochemical Characterization of a Widespread Enterobacterial Peroxidase Encapsulin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin.Communications biology · 2024Article
- 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
- Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii.Protein science : a publication of the Protein Society · 2024Article
- The oligomeric states of dye-decolorizing peroxidases from Streptomyces lividans and their implications for mechanism of substrate oxidation.Protein science : a publication of the Protein Society · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.bioRxiv : the preprint server for biology · 2024Article
- PMCNA_RS00975 activates NF-κB and ERK1/2 through TLR2 and contributes to the virulence ofFrontiers in cellular and infection microbiology · 2024Article
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Abstract
Encapsulins are self-assembling protein nanocompartments capable of selectively encapsulating dedicated cargo proteins, including enzymes involved in iron storage, sulfur metabolism, and stress resistance. They represent a unique compartmentalization strategy used by many pathogens to facilitate specialized metabolic capabilities. Encapsulation is mediated by specific cargo protein motifs known as targeting peptides (TPs), though the structural basis for encapsulation of the largest encapsulin cargo class, dye-decolorizing peroxidases (DyPs), is currently unknown. Here, we characterize a DyP-containing encapsulin from the enterobacterial pathogen Klebsiella pneumoniae. By combining cryo-electron microscopy with TP and TP-binding site mutagenesis, we elucidate the molecular basis for cargo encapsulation. TP binding is mediated by cooperative hydrophobic and ionic interactions as well as shape complementarity. Our results expand the molecular understanding of enzyme encapsulation inside protein nanocompartments and lay the foundation for rationally modulating encapsulin cargo loading for biomedical and biotechnological applications.
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