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High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
Journal
Acta Crystallographica Section F-Structural Biology Communications
Date Issued
2020
Author(s)
Liyana Azmi
Eilis C. Bragginton
Ian T. Cadby
Olwyn Byron
Andrew J. Roe
Andrew L. Lovering
Mads Gabrielsen
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.
Keywords: alcohol dehydrogenase; AdhE; Escherichia coli
Keywords: alcohol dehydrogenase; AdhE; Escherichia coli
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High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.pdf
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High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE
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1.35 MB
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Adobe PDF
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