8W4J

Cryo-EM structure of the KLHL22 E3 ligase bound to human glutamate dehydrogenase I

8W4J の概要

• エントリーDOI: 10.2210/pdb8w4j/pdb
• EMDBエントリー: 37235 37247 37266
• 分子名称: Glutamate dehydrogenase 1, mitochondrial, Kelch-like protein 22 (2 entities in total)
• 機能のキーワード: e3 ligase, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 512373.66

構造登録者

Su, M.-Y.,Su, M.-Y. (登録日: 2023-08-24, 公開日: 2023-11-01, 最終更新日: 2023-11-22)

主引用文献

Teng, F.,Wang, Y.,Liu, M.,Tian, S.,Stjepanovic, G.,Su, M.Y.
Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzyme.
Structure, 31:1431-, 2023

PubMed Abstract: 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.

PubMed: 37788672
DOI: 10.1016/j.str.2023.09.002

実験手法

ELECTRON MICROSCOPY (3.06 Å)