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Structure paper

TitleStructures of the 26S proteasome in complex with cochaperone Bag1
Journal, issue, pagesTo Be Published
Publish dateNov 14, 2024 (structure data deposition date)
AuthorsMaestro-Lopez M / Cheng TC / Muntaner J / Menendez M / Alonso M / Schweitzer A / Cuellar J / Valpuesta JM / Sakata E
External linksSearch PubMed
MethodsEM (single particle)
Resolution3.5 - 6.2 Å
Structure data

52097

9heu

EMDB-52097, PDB-9heu:
Co-chaperone Bag1-bound human 26S proteasome in SBAG1 state
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-52193: Co-chaperone Bag1-bound human 26S proteasome in SBAG2 state
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-52194: Co-chaperone Bag1-bound human 26S proteasome in SBAG3 state
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-52195: Hsp70-NBD:Bag1:Rpn1 ternary complex class 1
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-52196: Hsp70-NBD:Bag1:Rpn1 ternary complex class 2
Method: EM (single particle) / Resolution: 6.2 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Protein degradation / protease / AAA+ ATPase / Hsp70 / cochaperone / Bag1 / Complex / ubiquitin

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