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

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 t...

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Detalles Bibliográficos
Autores principales: Azmi, Liyana, Bragginton, Eilis C., Cadby, Ian T., Byron, Olwyn, Roe, Andrew J., Lovering, Andrew L., Gabrielsen, Mads
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2020
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470043/
https://www.ncbi.nlm.nih.gov/pubmed/32880589
http://dx.doi.org/10.1107/S2053230X20010237
Descripción
Sumario: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.

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