+検索条件
-Structure paper
タイトル | Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling. |
---|---|
ジャーナル・号・ページ | Commun Biol, Vol. 3, Issue 1, Page 298, Year 2020 |
掲載日 | 2020年6月10日 |
著者 | Gijeong Kim / Jinsol Yang / Juwon Jang / Jin-Seok Choi / Andrew J Roe / Olwyn Byron / Chaok Seok / Ji-Joon Song / |
PubMed 要旨 | 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 ...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. |
リンク | Commun Biol / PubMed:32523125 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.45 Å |
構造データ | EMDB-30220, PDB-7bvp: |
化合物 | ChemComp-NAD: ChemComp-ZN: |
由来 |
|
キーワード | OXIDOREDUCTASE / Spirosome / Aldehyde dehydrogenase / Alcohol dehydrogenase / NADH / HYDROLASE |