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TitleStructure of the human UBR5 E3 ubiquitin ligase.
Journal, issue, pagesStructure, Vol. 31, Issue 5, Page 541-552.e4, Year 2023
Publish dateMay 4, 2023
AuthorsFeng Wang / Qing He / Wenhu Zhan / Ziqi Yu / Efrat Finkin-Groner / Xiaojing Ma / Gang Lin / Huilin Li /
PubMed AbstractThe human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 functions like an ...The human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 functions like an oncoprotein to promote cancer growth and metastasis. Here, we report that UBR5 assembles into a dimer and a tetramer. Our cryoelectron microscopy (cryo-EM) structures reveal that two crescent-shaped UBR5 monomers assemble head to tail to form the dimer, and two dimers bind face to face to form the cage-like tetramer with all four catalytic HECT domains facing the central cavity. Importantly, the N-terminal region of one subunit and the HECT of the other form an "intermolecular jaw" in the dimer. We show the jaw-lining residues are important for function, suggesting that the intermolecular jaw functions to recruit ubiquitin-loaded E2 to UBR5. Further work is needed to understand how oligomerization regulates UBR5 ligase activity. This work provides a framework for structure-based anticancer drug development and contributes to a growing appreciation of E3 ligase diversity.
External linksStructure / PubMed:37040767 / PubMed Central
MethodsEM (single particle)
Resolution2.66 - 3.5 Å
Structure data

27201

8d4x

EMDB-27201, PDB-8d4x:
Structure of the human UBR5 HECT-type E3 ubiquitin ligase in a dimeric form
Method: EM (single particle) / Resolution: 2.8 Å

27822

8e0q

EMDB-27822, PDB-8e0q:
Structure of the human UBR5 HECT-type E3 ubiquitin ligase in a C2 symmetric dimeric form
Method: EM (single particle) / Resolution: 2.66 Å

28646

8ewi

EMDB-28646, PDB-8ewi:
Structure of the human UBR5 HECT-type E3 ubiquitin ligase in a tetrameric form
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / HECT / E3 ligase / Dimer

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