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-Structure paper
タイトル | Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 1426, Year 2020 |
掲載日 | 2020年3月18日 |
著者 | Pauline Pony / Chiara Rapisarda / Laurent Terradot / Esther Marza / Rémi Fronzes / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:32188856 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 3.4 - 5.0 Å |
構造データ | EMDB-10551, PDB-6tqh: EMDB-10552: EMDB-10555, PDB-6tqm: EMDB-10631: |
化合物 | ChemComp-NAD: ChemComp-FE: ChemComp-NAI: |
由来 |
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キーワード | OXIDOREDUCTASE / bacterial metabolism |