8OHS

Core-binding domain of fungal E3-binding domain bound to the native pyruvate dehydrogenase E2 core

8OHS の概要

• エントリーDOI: 10.2210/pdb8ohs/pdb
• EMDBエントリー: 14331 16884
• 分子名称: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial, Pyruvate dehydrogenase X component (2 entities in total)
• 機能のキーワード: complex, metabolism, mitochondria, transferase
• 由来する生物種: Neurospora crassa; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 426704.57

構造登録者

Forsberg, B.O. (登録日: 2023-03-21, 公開日: 2023-04-26, 最終更新日: 2024-07-24)

主引用文献

Forsberg, B.O.
The structure and evolutionary diversity of the fungal E3-binding protein.
Commun Biol, 6:480-480, 2023

PubMed Abstract: The pyruvate dehydrogenase complex (PDC) is a central metabolic enzyme in all living cells composed majorly of E1, E2, and E3. Tight coupling of their reactions makes each component essential, so that any loss impacts oxidative metabolism pathologically. E3 retention is mediated by the E3-binding protein (E3BP), which is here resolved within the PDC core from N.crassa, resolved to 3.2Å. Fungal and mammalian E3BP are shown to be orthologs, arguing E3BP as a broadly eukaryotic gene. Fungal E3BP architectures predicted from sequence data and computational models further bridge the evolutionary distance between N.crassa and humans, and suggest discriminants for E3-specificity. This is confirmed by similarities in their respective E3-binding domains, where an interaction previously not described is also predicted. This provides evolutionary parallels for a crucial interaction human metabolism, an interaction specific to fungi that can be targeted, and an example of protein evolution following gene neofunctionalization.

PubMed: 37137945
DOI: 10.1038/s42003-023-04854-7

実験手法

ELECTRON MICROSCOPY (4.1 Å)