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)

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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 > Institute of Infection Immunity and Inflammation
College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
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

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