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Single particle cryo-EM dataset of the Vairimorpha necatrix 26S proteasome from sporoplasms

ABSTRACT:

SUBMITTER: Nathan Jespersen

PROVIDER: EMPIAR-11121 | biostudies-other |

REPOSITORIES: biostudies-other

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Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores.

Jespersen Nathan N Ehrenbolger Kai K Winiger Rahel R RR Svedberg Dennis D Vossbrinck Charles R CR Barandun Jonas J

Nature communications 20221115 1

Proteasomes play an essential role in the life cycle of intracellular pathogens with extracellular stages by ensuring proteostasis in environments with limited resources. In microsporidia, divergent parasites with extraordinarily streamlined genomes, the proteasome complexity and structure are unknown, which limits our understanding of how these unique pathogens adapt and compact essential eukaryotic complexes. We present cryo-electron microscopy structures of the microsporidian 20S and 26S prot ...[more]

PMID: 36379934

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