Author
Listed:
- 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)
KTH Royal Institute of Technology
Karolinska Institutet)
- Hans Hebert
(KTH Royal Institute of Technology
Karolinska Institutet)
- Andrew J. Roe
(University of Glasgow)
- Olwyn Byron
(University of Glasgow)
- Ji-Joon Song
(Korea Advanced Institute of Science and Technology (KAIST))
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.
Suggested Citation
Gijeong Kim & Liyana Azmi & Seongmin Jang & Taeyang Jung & Hans Hebert & Andrew J. Roe & Olwyn Byron & Ji-Joon Song, 2019.
"Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity,"
Nature Communications, Nature, vol. 10(1), pages 1-11, December.
Handle:
RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12427-8
DOI: 10.1038/s41467-019-12427-8
Download full text from publisher
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12427-8. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.