1. High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
- Author
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Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, and Gabrielsen M
- Subjects
- Alcohol Dehydrogenase genetics, Alcohol Dehydrogenase metabolism, Aldehyde Oxidoreductases genetics, Aldehyde Oxidoreductases metabolism, Amino Acid Sequence, Catalytic Domain, Cations, Divalent, Cloning, Molecular, Crystallography, X-Ray, Escherichia coli O157 genetics, Escherichia coli Proteins genetics, Escherichia coli Proteins metabolism, Gene Expression, Genetic Vectors chemistry, Genetic Vectors metabolism, Iron metabolism, Models, Molecular, NAD metabolism, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Subunits genetics, Protein Subunits metabolism, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Alcohol Dehydrogenase chemistry, Aldehyde Oxidoreductases chemistry, Escherichia coli O157 enzymology, Escherichia coli Proteins chemistry, Iron chemistry, NAD chemistry, Protein Subunits chemistry
- 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., (open access.)
- Published
- 2020
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