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

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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 angstrom 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.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2019-10
Language
English
Article Type
Article
Citation

NATURE COMMUNICATIONS, v.10

ISSN
2041-1723
DOI
10.1038/s41467-019-12427-8
URI
http://hdl.handle.net/10203/268038
Appears in Collection
BS-Journal Papers(저널논문)
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