6AHC

Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity

6AHC の概要

• エントリーDOI: 10.2210/pdb6ahc/pdb
• EMDBエントリー: 9623
• 分子名称: Aldehyde-alcohol dehydrogenase (1 entity in total)
• 機能のキーワード: acetyl coa, ethanol, regulation, high-order structure, hydrolase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 771106.06

構造登録者

Kim, G.,Song, J.J. (登録日: 2018-08-17, 公開日: 2019-08-21, 最終更新日: 2024-03-27)

主引用文献

Kim, G.,Azmi, L.,Jang, S.,Jung, T.,Hebert, H.,Roe, A.J.,Byron, O.,Song, J.J.
Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Nat Commun, 10:4527-4527, 2019

PubMed Abstract: Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 Å resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity.

PubMed: 31586059
DOI: 10.1038/s41467-019-12427-8

実験手法

ELECTRON MICROSCOPY (3.45 Å)