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; Ji-Joon Song

doi:10.1038/s41467-019-12427-8

Nature Communications (Oct 2019)

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,
Ji-Joon Song

Affiliations

Gijeong Kim: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST)
Liyana Azmi: Institute of Infection, Immunity and Inflammation, University of Glasgow
Seongmin Jang: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST)
Taeyang Jung: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST)
Hans Hebert: School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology
Andrew J. Roe: Institute of Infection, Immunity and Inflammation, University of Glasgow
Olwyn Byron: School of Life Sciences, University of Glasgow
Ji-Joon Song: Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST)

DOI: https://doi.org/10.1038/s41467-019-12427-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

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Aldehyde-alcohol dehydrogenase (AdhE) converts acetyl-CoA to ethanol and plays an important role in bacterial fermentation. Here the authors present the 3.5 Å cryo-EM structure of full-length E. coli AdhE, which reveals a right-handed helical spirosome structure and they show that the helical structure is required for AdhE activity.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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