7DAG

Vibrio cholera aldehyde-alcohol dehrogenase

7DAG の概要

• エントリーDOI: 10.2210/pdb7dag/pdb
• EMDBエントリー: 30625 9623
• 分子名称: Aldehyde-alcohol dehydrogenase (1 entity in total)
• 機能のキーワード: enzyme, fermentation, alcohol, aldehyde, oxidoreductase
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 770769.94

構造登録者

Cho, S.,Cho, C.,Song, J.,Kim, G. (登録日: 2020-10-16, 公開日: 2020-12-30, 最終更新日: 2024-03-27)

主引用文献

Cho, S.,Kim, G.,Song, J.J.,Cho, C.
Cryo-EM structure of Vibrio cholerae aldehyde-alcohol dehydrogenase spirosomes.
Biochem.Biophys.Res.Commun., 536:38-44, 2020

PubMed Abstract: Aldehyde-alcohol dehydrogenase (AdhE) is a metabolic enzyme and virulence factor in bacteria. E. coli AdhE (eAdhE) multimerizes into spirosomes that are essential for enzymatic activity. However, it is unknown whether AdhE structure is conserved in divergent bacteria. Here, we present the cryo-EM structure of AdhE (vAdhE) from Vibrio cholerae to 4.31 Å resolution. Overall, vAdhE spirosomes are similar to eAdhE with conserved subunit arrangement. However, divergences in key oligomerization residues cause vAdhE to form labile spirosomes with lower enzymatic activity. Mutating the vAdhE oligomerization interface to mimic eAdhE increases spirosome stability and enzymatic activity to levels comparable to eAdhE. These results support the generality of AdhE spirosome structures, and provide a structural basis to target vAdhE to attenuate bacterial virulence.

PubMed: 33360541
DOI: 10.1016/j.bbrc.2020.12.040

実験手法

ELECTRON MICROSCOPY (4.37 Å)