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TitleCryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme.
Journal, issue, pagesStructure, Vol. 31, Issue 11, Page 1431-11440.e5, Year 2023
Publish dateNov 2, 2023
AuthorsFei Teng / Yang Wang / Ming Liu / Shuyun Tian / Goran Stjepanovic / Ming-Yuan Su /
PubMed AbstractCULLIN-RING ligases constitute the largest group of E3 ubiquitin ligases. While some CULLIN family members recruit adapters before engaging further with different substrate receptors, homo-dimeric ...CULLIN-RING ligases constitute the largest group of E3 ubiquitin ligases. While some CULLIN family members recruit adapters before engaging further with different substrate receptors, homo-dimeric BTB-Kelch family proteins combine adapter and substrate receptor into a single polypeptide for the CULLIN3 family. However, the entire structural assembly and molecular details have not been elucidated to date. Here, we present a cryo-EM structure of the CULLIN3 in complex with Kelch-like protein 22 (KLHL22) and a mitochondrial glutamate dehydrogenase complex I (GDH1) at 3.06 Å resolution. The structure adopts a W-shaped architecture formed by E3 ligase dimers. Three CULLIN3 dimers were found to be dynamically associated with a single GDH1 hexamer. CULLIN3 ligase mediated the polyubiquitination of GDH1 in vitro. Together, these results enabled the establishment of a structural model for understanding the complete assembly of BTB-Kelch proteins with CULLIN3 and how together they recognize oligomeric substrates and target them for ubiquitination.
External linksStructure / PubMed:37788672
MethodsEM (single particle)
Resolution2.59 - 3.67 Å
Structure data

37235

8kgy

EMDB-37235, PDB-8kgy:
Human glutamate dehydrogenase I
Method: EM (single particle) / Resolution: 2.59 Å

37247

8khp

EMDB-37247, PDB-8khp:
CULLIN3-KLHL22-RBX1 E3 ligase
Method: EM (single particle) / Resolution: 3.67 Å

37266

8w4j

EMDB-37266, PDB-8w4j:
Cryo-EM structure of the KLHL22 E3 ligase bound to human glutamate dehydrogenase I
Method: EM (single particle) / Resolution: 3.06 Å

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / dehydrogenase / STRUCTURAL PROTEIN / E3 ligase

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