[논문]Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling

Kim, Gijeong; Yang, Jinsol; Jang, Juwon; Choi, Jin-Seok; Roe, Andrew J.; Byron, Olwyn; Seok, Chaok; Song, Ji-Joon

doi:10.1038/s42003-020-1030-1

[해외논문] Aldehyde-alcohol dehydrogenase undergoes structural transition to form extended spirosomes for substrate channeling 원문보기

Communications biology, v.3 no.1, 2020년, pp.298 -

Kim, Gijeong (Department of Biological Sciences, KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141 Korea) , Yang, Jinsol (Department of Chemistry, Seoul National University, Seoul, 08826 Korea) , Jang, Juwon (Department of Biological Sciences, KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141 Korea) , Choi, Jin-Seok (Analysis Center for Research Advancement, KAIST, Daejeon, 34141 Korea) , Roe, Andrew J. (Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow, G12 8QQ Scotland UK) , Byron, Olwyn (School of Life Sciences, University of Glasgow, Glasgow, G12 8QQ Scotland UK) , Seok, Chaok (Department of Chemistry, Seoul National University, Seoul, 08826 Korea) , Song, Ji-Joon (Department of Biological Sciences, KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141 Korea)

Abstract ▼ AI-Helper

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.Using cryo-EM, Kim et al. show that aldehyde-alcohol dehydrogenase (AdhE) spirosomes undergo structural transition from compact to extended conformation from substrate binding. This transition opens up the substrate channel that transports the reaction intermediates to the next catalytic site.

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