Related Experiment Video
Updated: Dec 10, 2025

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
Liyana Azmi1, Eilis C Bragginton2, Ian T Cadby2
1Institute of Infection, Immunity and Inflammation, University of Glasgow, University Avenue, Glasgow G12 8QQ, United Kingdom.
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.
Related Concept Videos
ATP Synthase: Structure
Structures of Aldehydes and Ketones
In aldehydes (Figures 1a and 1b), the...
Aldehydes and Ketones with Alcohols: Hemiacetal Formation
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Electron Transport Chain: Complex III and IV
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

