Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity

Gijeong Kim, Liyana Azmi, Seongmin Jang, Taeyang Jung, Hans Hebert, Andrew J. Roe, Olwyn Byron and Ji-Joon Song ()
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Gijeong Kim: Korea Advanced Institute of Science and Technology (KAIST)
Liyana Azmi: University of Glasgow
Seongmin Jang: Korea Advanced Institute of Science and Technology (KAIST)
Taeyang Jung: Korea Advanced Institute of Science and Technology (KAIST)
Hans Hebert: KTH Royal Institute of Technology
Andrew J. Roe: University of Glasgow
Olwyn Byron: University of Glasgow
Ji-Joon Song: Korea Advanced Institute of Science and Technology (KAIST)

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-12427-8

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