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

Azmi, L., Bragginton, E. C., Cadby, I. T., Byron, O. , Roe, A. J. , Lovering, A. L. and Gabrielsen, M. (2020) High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE. Acta Crystallographica. Section F: Structural Biology Communications, 76(9), pp. 414-421. (doi: 10.1107/S2053230X20010237)

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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Gabrielsen, Dr Mads and Roe, Professor Andrew and Byron, Professor Olwyn
• Authors: Azmi, L., Bragginton, E. C., Cadby, I. T., Byron, O., Roe, A. J., Lovering, A. L., and Gabrielsen, M.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity; College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Journal Name: Acta Crystallographica. Section F: Structural Biology Communications
• Publisher: Wiley
• ISSN: 2053-230X
• ISSN (Online): 2053-230X
• Published Online: 19 August 2020
• Copyright Holders: Copyright © 2020 The Authors
• First Published: First published in Acta Crystallographica. Section F: Structural Biology Communications 76(9):414-421
• Publisher Policy: Reproduced under a Creative Commons licence