7DAG

Vibrio cholera aldehyde-alcohol dehrogenase

Summary for 7DAG

• Entry DOI: 10.2210/pdb7dag/pdb
• EMDB information: 30625 9623
• Descriptor: Aldehyde-alcohol dehydrogenase (1 entity in total)
• Functional Keywords: enzyme, fermentation, alcohol, aldehyde, oxidoreductase
• Biological source: Vibrio cholerae
• Total number of polymer chains: 8
• Total formula weight: 770769.94

Authors

Cho, S.,Cho, C.,Song, J.,Kim, G. (deposition date: 2020-10-16, release date: 2020-12-30, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4.37 Å)