Abstract
The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 Å resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.
| Original language | English |
|---|---|
| Pages (from-to) | 414-421 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section F: Structural Biology Communications |
| Volume | 76 |
| DOIs | |
| Publication status | Published - 1 Sept 2020 |
Bibliographical note
Funding Information:We thank Diamond Light Source for the MX and SAXS beamtime (MX12112 and MX11651, respectively) and the BL21 beamline scientists for excellent scientific support.
Publisher Copyright:
© 2020 International Union of Crystallography. All rights reserved.
Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
Keywords
- AdhE
- alcohol dehydrogenase
- Escherichia coli
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics
Fingerprint
Dive into the research topics of 'High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE'. Together they form a unique fingerprint.Equipment
-
Birmingham Environment for Academic Research (BEAR)
Facility/equipment: Equipment