The structure and activity of the glutathione reductase from Streptococcus pneumoniae.
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Binding Sites
Biocatalysis
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Glutathione
/ chemistry
Glutathione Reductase
/ chemistry
Kinetics
Models, Molecular
NADP
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Recombinant Proteins
/ chemistry
Streptococcus pneumoniae
/ chemistry
Structural Homology, Protein
Substrate Specificity
Streptococcus pneumoniae
X-ray crystallography
glutathione reductase
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 Jan 2019
01 Jan 2019
Historique:
received:
02
07
2018
accepted:
20
11
2018
entrez:
4
1
2019
pubmed:
4
1
2019
medline:
13
4
2019
Statut:
ppublish
Résumé
The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 Å resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel β-sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for K
Identifiants
pubmed: 30605126
pii: S2053230X18016527
doi: 10.1107/S2053230X18016527
pmc: PMC6317452
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Proteins
0
NADP
53-59-8
Glutathione Reductase
EC 1.8.1.7
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
54-61Subventions
Organisme : National Health and Medical Research Council
ID : GNT1080784
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