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TitleAldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 4527, Year 2019
Publish dateOct 4, 2019
AuthorsGijeong Kim / Liyana Azmi / Seongmin Jang / Taeyang Jung / Hans Hebert / Andrew J Roe / Olwyn Byron / Ji-Joon Song /
PubMed AbstractAldehyde-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- ...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.
External linksNat Commun / PubMed:31586059 / PubMed Central
MethodsEM (single particle)
Resolution3.45 Å
Structure data

EMDB-9623, PDB-6ahc:
Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity
Method: EM (single particle) / Resolution: 3.45 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsHYDROLASE / acetyl CoA / ethanol / regulation / high-order structure

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