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Structure paper

TitleAllosteric control of Ubp6 and the proteasome via a bidirectional switch.
Journal, issue, pagesNat Commun, Vol. 13, Page 838, Year 2022
Publish dateDec 23, 2021 (structure data deposition date)
AuthorsHung KYS / Klumpe S / Eisele MR / Elsasser S / Tian G / Sun S / Moroco JA / Cheng TC / Joshi T / Seibel T ...Hung KYS / Klumpe S / Eisele MR / Elsasser S / Tian G / Sun S / Moroco JA / Cheng TC / Joshi T / Seibel T / Van Dalen D / Feng XH / Lu Y / Ovaa H / Engen JR / Lee BH / Rudack T / Sakata E / Finley D
External linksNat Commun / Search PubMed
MethodsEM (single particle)
Resolution7.0 Å
Structure data

14083

7qo4

EMDB-14083, PDB-7qo4:
26S proteasome WT-Ubp6-UbVS complex in the si state (ATPases, Rpn1, Ubp6, and UbVS)
Method: EM (single particle) / Resolution: 7.0 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • baker's yeast (brewer's yeast)
  • homo sapiens (human)
KeywordsMOTOR PROTEIN / Proteasome / UBP6 / Ubiquitin / Allostery

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