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TitleCryo-EM Reveals Unanchored M1-Ubiquitin Chain Binding at hRpn11 of the 26S Proteasome.
Journal, issue, pagesStructure, Vol. 28, Issue 11, Page 1206-11217.e4, Year 2020
Publish dateNov 3, 2020
AuthorsXiang Chen / Zachary Dorris / Dan Shi / Rick K Huang / Htet Khant / Tara Fox / Natalia de Val / Dewight Williams / Ping Zhang / Kylie J Walters /
PubMed AbstractThe 26S proteasome is specialized for regulated protein degradation and formed by a dynamic regulatory particle (RP) that caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. ...The 26S proteasome is specialized for regulated protein degradation and formed by a dynamic regulatory particle (RP) that caps a hollow cylindrical core particle (CP) where substrates are proteolyzed. Its diverse substrates unify as proteasome targets by ubiquitination. We used cryogenic electron microscopy (cryo-EM) to study how human 26S proteasome interacts with M1-linked hexaubiquitin (M1-Ub) unanchored to a substrate and E3 ubiquitin ligase E6AP/UBE3A. Proteasome structures are available with model substrates extending through the RP ATPase ring and substrate-conjugated K63-linked ubiquitin chains present at inhibited deubiquitinating enzyme hRpn11 and the nearby ATPase hRpt4/hRpt5 coiled coil. In this study, we find M1-Ub at the hRpn11 site despite the absence of conjugated substrate, indicating that ubiquitin binding at this location does not require substrate interaction with the RP. Moreover, unanchored M1-Ub binds to this hRpn11 site of the proteasome with the CP gating residues in both the closed and opened conformational states.
External linksStructure / PubMed:32783951 / PubMed Central
MethodsEM (single particle)
Resolution4.1 - 6.75 Å
Structure data

21691

6wjd

EMDB-21691, PDB-6wjd:
SA-like state of human 26S Proteasome with non-cleavable M1-linked hexaubiquitin and E3 ubiquitin ligase E6AP/UBE3A
Method: EM (single particle) / Resolution: 4.8 Å

21696

6wjn

EMDB-21696, PDB-6wjn:
SD-like state of human 26S Proteasome with non-cleavable M1-linked hexaubiquitin and E3 ubiquitin ligase E6AP/UBE3A
Method: EM (single particle) / Resolution: 5.7 Å

EMDB-21697:
SA-like state of human 26S proteasome in complex with non-cleavable M1-linked hexaubiquitin
Method: EM (single particle) / Resolution: 5.8 Å

EMDB-21698:
SD-like state of human 26S proteasome in complex with non-cleavable M1-linked hexaubiquitin
Method: EM (single particle) / Resolution: 5.96 Å

EMDB-21699:
SA-like state of human 26S proteasome in complex with non-cleavable M1-linked hexaubiquitin
Method: EM (single particle) / Resolution: 6.75 Å

EMDB-21700:
SD-like state of human 26S proteasome in complex with non-cleavable M1-linked hexaubiquitin
Method: EM (single particle) / Resolution: 6.47 Å

EMDB-21704:
Global map of human 26S Proteasome with non-cleavable M1-linked hexaubiquitin and E3 ubiquitin ligase E6AP/UBE3A
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

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

Source
  • homo sapiens (human)
KeywordsHYDROLASE/PROTEIN BINDING / 26S protease / ubiquitin / complex / subunit / HYDROLASE-PROTEIN BINDING complex

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