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TitleFilamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 1426, Year 2020
Publish dateMar 18, 2020
AuthorsPauline Pony / Chiara Rapisarda / Laurent Terradot / Esther Marza / Rémi Fronzes /
PubMed AbstractAcetaldehyde-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 ...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.
External linksNat Commun / PubMed:32188856 / PubMed Central
MethodsEM (single particle) / EM (helical sym.)
Resolution3.4 - 5.0 Å
Structure data

10551

6tqh

EMDB-10551, PDB-6tqh:
Escherichia coli AdhE structure in its extended conformation
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-10552:
Helical reconstruction of AdhE from Escherichia coli in its extended conformation
Method: EM (helical sym.) / Resolution: 3.9 Å

10555

6tqm

EMDB-10555, PDB-6tqm:
Escherichia coli AdhE structure in its compact conformation
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-10631:
Helical reconstruction of AdhE from Escherichia coli in its compact conformation
Method: EM (helical sym.) / Resolution: 5.0 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-FE:
Unknown entry

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

Source
  • escherichia coli (E. coli)
  • Escherichia coli (strain K12) (bacteria)
  • escherichia coli k-12 (bacteria)
KeywordsOXIDOREDUCTASE / bacterial metabolism

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