6TQH

Escherichia coli AdhE structure in its extended conformation

Summary for 6TQH

• Entry DOI: 10.2210/pdb6tqh/pdb
• EMDB information: 10551
• Descriptor: Aldehyde-alcohol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, FE (III) ION (3 entities in total)
• Functional Keywords: bacterial metabolism, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 387741.86

Authors

Fronzes, R.,Pony, P. (deposition date: 2019-12-16, release date: 2020-06-03, Last modification date: 2024-05-22)

Primary citation

Pony, P.,Rapisarda, C.,Terradot, L.,Marza, E.,Fronzes, R.
Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.
Nat Commun, 11:1426-1426, 2020

PubMed Abstract: Acetaldehyde-alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. It is found as an oligomeric form called spirosomes, for which the function remains elusive. Here, we use cryo-electron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We show that spirosomes contain active AdhE monomers, and that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity.

PubMed: 32188856
DOI: 10.1038/s41467-020-15214-y

Experimental method

ELECTRON MICROSCOPY (3.4 Å)