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TitleCryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps.
Journal, issue, pagesStructure, Vol. 33, Issue 10, Page 1643-11648.e1, Year 2025
Publish dateOct 2, 2025
AuthorsSofia Lövestam / Sjors H W Scheres /
PubMed AbstractThe vault protein is expressed in most eukaryotic cells, where it is assembled on polyribosomes into large hollow barrel-shaped complexes. Despite its widespread and abundant presence in cells, the ...The vault protein is expressed in most eukaryotic cells, where it is assembled on polyribosomes into large hollow barrel-shaped complexes. Despite its widespread and abundant presence in cells, the biological function of the vault remains unclear. In this study, we describe the cryo-EM structure of vault particles that were imaged as a contamination of a preparation to extract tau filaments from brain tissue of an individual with progressive supranuclear palsy (PSP). We identify a mechanism of symmetry mismatch at the caps of the vault, from 39-fold to 13-fold symmetry, where two out of three monomers are sequentially excluded from the cap, resulting in a narrow, greasy pore at the tip of the vault. Our structure offers valuable insights for engineering carboxy-terminal modifications of the major vault protein (MVP) for potential therapeutic applications.
External linksStructure / PubMed:40803316
MethodsEM (single particle)
Resolution3.1 - 3.6 Å
Structure data

53805

9r86

EMDB-53805, PDB-9r86:
Major Vault Protein from Human Brain
Method: EM (single particle) / Resolution: 3.1 Å

53806

9r87

EMDB-53806, PDB-9r87:
Cap of the vault protein from Human Brain
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / Complex / Vault / large protein / cap

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