8X02

E2 core of 2-oxoglutarate dehydrogenase complex

8X02 の概要

• エントリーDOI: 10.2210/pdb8x02/pdb
• EMDBエントリー: 37965
• 分子名称: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (1 entity in total)
• 機能のキーワード: structure of mitochondrial enzyme complex, transferase
• 由来する生物種: Sus scrofa (pig)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1176923.62

構造登録者

Zhang, S.S.,Zhang, Y.T. (登録日: 2023-11-03, 公開日: 2024-10-30)

主引用文献

Zhang, Y.,Chen, M.,Chen, X.,Zhang, M.,Yin, J.,Yang, Z.,Gao, X.,Zhang, S.,Yang, M.
Molecular architecture of the mammalian 2-oxoglutarate dehydrogenase complex.
Nat Commun, 15:8407-8407, 2024

PubMed Abstract: The 2-oxoglutarate dehydrogenase complex (OGDHc) orchestrates a critical reaction regulating the TCA cycle. Although the structure of each OGDHc subunit has been solved, the architecture of the intact complex and inter-subunit interactions still remain unknown. Here we report the assembly of native, intact OGDHc from Sus scrofa heart tissue using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), and subtomogram averaging (STA) to discern native structures of the whole complex and each subunit. Our cryo-EM analyses revealed the E2o cubic core structure comprising eight homotrimers at 3.3-Å resolution. More importantly, the numbers, positions and orientations of each OGDHc subunit were determined by cryo-ET and the STA structures of the core were resolved at 7.9-Å with the peripheral subunits reaching nanometer resolution. Although the distribution of the peripheral subunits E1o and E3 vary among complexes, they demonstrate a certain regularity within the position and orientation. Moreover, we analyzed and validated the interactions between each subunit, and determined the flexible binding mode for E1o, E2o and E3, resulting in a proposed model of Sus scrofa OGDHc. Together, our results reveal distinctive factors driving the architecture of the intact, native OGDHc.

PubMed: 39333186
DOI: 10.1038/s41467-024-52792-7

実験手法

ELECTRON MICROSCOPY (3.3 Å)