High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.
Alcohol Dehydrogenase
/ chemistry
Aldehyde Oxidoreductases
/ chemistry
Amino Acid Sequence
Catalytic Domain
Cations, Divalent
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli O157
/ enzymology
Escherichia coli Proteins
/ chemistry
Gene Expression
Genetic Vectors
/ chemistry
Iron
/ chemistry
Models, Molecular
NAD
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Protein Subunits
/ chemistry
Recombinant Proteins
/ chemistry
AdhE
Escherichia coli
alcohol dehydrogenase
Journal
Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319
Informations de publication
Date de publication:
01 Sep 2020
01 Sep 2020
Historique:
received:
20
01
2020
accepted:
23
07
2020
entrez:
4
9
2020
pubmed:
4
9
2020
medline:
7
7
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32880589
pii: S2053230X20010237
doi: 10.1107/S2053230X20010237
pmc: PMC7470043
doi:
Substances chimiques
Cations, Divalent
0
Escherichia coli Proteins
0
Protein Subunits
0
Recombinant Proteins
0
NAD
0U46U6E8UK
Iron
E1UOL152H7
Alcohol Dehydrogenase
EC 1.1.1.1
adhE protein, E coli
EC 1.1.1.1
Aldehyde Oxidoreductases
EC 1.2.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
414-421Informations de copyright
open access.
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