한빛사 논문
Gijeong Kim1, Liyana Azmi2, Seongmin Jang1, Taeyang Jung1,3,4, Hans Hebert3,4, Andrew J. Roe2, Olwyn Byron5 & Ji-Joon Song1,*
1 Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
2 Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8QQ Scotland, UK.
3 School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Novum SE-141 57, Sweden.
4 Department of Biosciences and Nutrition, Karolinska Institutet, S-141 83 Huddinge, Sweden.
5 School of Life Sciences, University of Glasgow, Glasgow G12 8QQ Scotland, UK.
*Correspondence to Ji-Joon Song
Abstract
Aldehyde-alcohol dehydrogenase (AdhE) is a key enzyme in bacterial fermentation, converting acetyl-CoA to ethanol, via two consecutive catalytic reactions. Here, we present a 3.5 Å resolution cryo-EM structure of full-length AdhE revealing a high-order spirosome architecture. The structure shows that the aldehyde dehydrogenase (ALDH) and alcohol dehydrogenase (ADH) active sites reside at the outer surface and the inner surface of the spirosome respectively, thus topologically separating these two activities. Furthermore, mutations disrupting the helical structure abrogate enzymatic activity, implying that formation of the spirosome structure is critical for AdhE activity. In addition, we show that this spirosome structure undergoes conformational change in the presence of cofactors. This work presents the atomic resolution structure of AdhE and suggests that the high-order helical structure regulates its enzymatic activity.
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