7BVP

AdhE spirosome in extended conformation

Summary for 7BVP

• Entry DOI: 10.2210/pdb7bvp/pdb
• Related: 6AHC
• EMDB information: 30220 9623
• Descriptor: Aldehyde-alcohol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION (3 entities in total)
• Functional Keywords: spirosome, aldehyde dehydrogenase, alcohol dehydrogenase, nadh, hydrolase, oxidoreductase
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 6
• Total formula weight: 586683.10

Authors

Kim, G.J.,Song, J.J. (deposition date: 2020-04-11, release date: 2020-06-24, Last modification date: 2024-03-27)

Primary citation

Kim, G.,Yang, J.,Jang, J.,Choi, J.S.,Roe, A.J.,Byron, O.,Seok, C.,Song, J.J.
Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling.
Commun Biol, 3:298-298, 2020

PubMed Abstract: Aldehyde-alcohol dehydrogenase (AdhE) is an enzyme responsible for converting acetyl-CoA to ethanol via acetaldehyde using NADH. AdhE is composed of two catalytic domains of aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH), and forms a spirosome architecture critical for AdhE activity. Here, we present the atomic resolution (3.43 Å) cryo-EM structure of AdhE spirosomes in an extended conformation. The cryo-EM structure shows that AdhE spirosomes undergo a structural transition from compact to extended forms, which may result from cofactor binding. This transition leads to access to a substrate channel between ALDH and ADH active sites. Furthermore, prevention of this structural transition by crosslinking hampers the activity of AdhE, suggesting that the structural transition is important for AdhE activity. This work provides a mechanistic understanding of the regulation mechanisms of AdhE activity via structural transition, and a platform to modulate AdhE activity for developing antibiotics and for facilitating biofuel production.

PubMed: 32523125
DOI: 10.1038/s42003-020-1030-1

Experimental method

ELECTRON MICROSCOPY (3.45 Å)