8U50

Klebsiella pneumoniae DyP peroxidase-loaded encapsulin shell

Summary for 8U50

• Entry DOI: 10.2210/pdb8u50/pdb
• EMDB information: 41905
• Descriptor: Klebsiella pneumoniae family 1 encapsulin shell (1 entity in total)
• Functional Keywords: encapsulin, nanocompartment, dyp peroxidase, virus like particle
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 28841.13

Authors

Andreas, M.P.,Jones, J.A.,Giessen, T.W. (deposition date: 2023-09-11, release date: 2024-04-24)

Primary citation

Jones, J.A.,Andreas, M.P.,Giessen, T.W.
Structural basis for peroxidase encapsulation inside the encapsulin from the Gram-negative pathogen Klebsiella pneumoniae.
Nat Commun, 15:2558-2558, 2024

PubMed 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.

PubMed: 38519509
DOI: 10.1038/s41467-024-46880-x

Experimental method

ELECTRON MICROSCOPY (2.52 Å)