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Structure paper

TitleMolecular basis for ubiquitin-independent substrate degradation by midnolin-proteasome
Journal, issue, pagesTo Be Published
Publish dateMar 13, 2025 (structure data deposition date)
AuthorsZhu C / Qin L
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.75 - 3.5 Å
Structure data

EMDB-63725: Focused refinement of 19S in the substrate-engaged human 26S proteasome bound to midnolin with RPT1 at top of spiral staircase
Method: EM (single particle) / Resolution: 3.34 Å

EMDB-63726: Consensus map of substrate-engaged human 26S proteasome bound to midnolin with RPT1 at top of spiral staircase
Method: EM (single particle) / Resolution: 2.75 Å

EMDB-63727: Consensus map of substrate-engaged human 26S proteasome bound to midnolin with RPT5 at top of spiral staircase
Method: EM (single particle) / Resolution: 2.93 Å

EMDB-63728: Focused refinement of 19S in the substrate-engaged human 26S proteasome bound to midnolin with RPT5 at top of spiral staircase
Method: EM (single particle) / Resolution: 3.44 Å

EMDB-63751: Consensus map of substrate-engaged human 26S proteasome bound to midnolin with RPT2 at top of spiral staircase
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-63752: Focused refinement of 19S in the substrate-engaged human 26S proteasome bound to midnolin with RPT2 at top of spiral staircase
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • Homo sapiens (human)

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