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TitleStructure and heterogeneity of a highly cargo-loaded encapsulin shell.
Journal, issue, pagesJ Struct Biol, Vol. 215, Issue 4, Page 108022, Year 2023
Publish dateAug 30, 2023
AuthorsSeokmu Kwon / Michael P Andreas / Tobias W Giessen /
PubMed AbstractEncapsulins are self-assembling protein nanocompartments able to selectively encapsulate dedicated cargo enzymes. Encapsulins are widespread across bacterial and archaeal phyla and are involved in ...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.
External linksJ Struct Biol / PubMed:37657675
MethodsEM (single particle)
Resolution2.53 Å
Structure data

41322

8tk7

EMDB-41322, PDB-8tk7:
Myxococcus xanthus EncA protein shell with compartmentalized SNAP-tag cargo protein
Method: EM (single particle) / Resolution: 2.53 Å

Source
  • myxococcus xanthus dk 1622 (bacteria)
  • homo sapiens (human)
KeywordsVIRUS LIKE PARTICLE / Encapsulin / nanocompartment

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