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High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2020 Sep 01; Vol. 76 (Pt 9), pp. 414-421. Date of Electronic Publication: 2020 Aug 19. - Publication Year :
- 2020
-
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.<br /> (open access.)
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 76
- Issue :
- Pt 9
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 32880589
- Full Text :
- https://doi.org/10.1107/S2053230X20010237