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

Autor:	Eilis C. Bragginton, Andrew L. Lovering, Liyana Azmi, Mads Gabrielsen, Olwyn Byron, Ian T. Cadby, Andrew J. Roe
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	Models Molecular Protein Conformation alpha-Helical Aldehyde dehydrogenase High resolution Gene Expression Alcohol medicine.disease_cause Crystallography X-Ray Biochemistry Research Communications chemistry.chemical_compound Structural Biology Catalytic Domain Cloning Molecular chemistry.chemical_classification 0303 health sciences biology integumentary system Escherichia coli Proteins Condensed Matter Physics Aldehyde Oxidoreductases Recombinant Proteins hormones hormone substitutes and hormone antagonists Protein Binding Cations Divalent Iron Genetic Vectors Biophysics Escherichia coli O157 03 medical and health sciences In vivo Genetics medicine Escherichia coli AdhE Protein Interaction Domains and Motifs Amino Acid Sequence Bifunctional 030304 developmental biology Alcohol dehydrogenase 030306 microbiology urogenital system Alcohol Dehydrogenase NAD Protein Subunits Enzyme chemistry biology.protein bacteria Protein Conformation beta-Strand Protein Multimerization
Zdroj:	Acta Crystallographica. Section F, Structural Biology Communications
ISSN:	2053-230X
Popis:	The crystal structure of the alcohol dehydrogenase domain of AdhE from Escherichia coli is reported. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd82fe826218aba4f8da4c5c3b0f855e http://europepmc.org/articles/PMC7470043 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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