High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE

Research output: Contribution to journalArticlepeer-review


  • Liyana Azmi
  • Olwyn Byron
  • Andrew J. Roe
  • Mads Gabrielsen

Colleges, School and Institutes

External organisations

  • University of Glasgow
  • CRUK Beatson Institute


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.

Bibliographic 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.


Original languageEnglish
Pages (from-to)414-421
Number of pages8
JournalActa Crystallographica Section F: Structural Biology Communications
Publication statusPublished - 1 Sep 2020


  • AdhE, alcohol dehydrogenase, Escherichia coli