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X-ray structure of Arthrobacter globiformis M30 ketose 3-epimerase for the production of d-allulose from d-fructose
- Source :
- Acta Crystallogr F Struct Biol Commun
- Publication Year :
- 2018
- Publisher :
- International Union of Crystallography, 2018.
-
Abstract
- The X-ray structure of ketose 3-epimerase from Arthrobacter globiformis M30, which was previously reported to be a D-allulose 3-epimerase (AgD-AE), was determined at 1.96 Å resolution. The crystal belonged to the hexagonal space group P6522, with unit-cell parameters a = b = 103.98, c = 256.53 Å. The structure was solved by molecular replacement using the structure of Mesorhizobium loti L-ribulose 3-epimerase (MlL-RE), which has 41% sequence identity, as a search model. A hexagonal crystal contained two molecules in the asymmetric unit, and AgD-AE formed a homotetramer with twofold symmetry. The overall structure of AgD-AE was more similar to that of MlL-RE than to the known structures of D-psicose (alternative name D-allulose) 3-epimerases (D-PEs or D-AEs), although AgD-AE and MlL-RE have different substrate specificities. Both AgD-AE and MlL-RE have long helices in the C-terminal region that would contribute to the stability of the homotetramer. AgD-AE showed higher enzymatic activity for L-ribulose than D-allulose; however, AgD-AE is stable and is a unique useful enzyme for the production of D-allulose from D-fructose.
- Subjects :
- 0301 basic medicine
Models, Molecular
Protein Conformation, alpha-Helical
Stereochemistry
Genetic Vectors
Pentoses
Biophysics
Gene Expression
Fructose
Crystallography, X-Ray
Biochemistry
Research Communications
Substrate Specificity
Crystal
03 medical and health sciences
Bacterial Proteins
Structural Biology
Catalytic Domain
Ketoses
Genetics
Escherichia coli
Molecule
Molecular replacement
Protein Interaction Domains and Motifs
Amino Acid Sequence
Arthrobacter
Cloning, Molecular
chemistry.chemical_classification
biology
Chemistry
Resolution (electron density)
Ketose
Mesorhizobium
Condensed Matter Physics
biology.organism_classification
Recombinant Proteins
Mesorhizobium loti
030104 developmental biology
Enzyme
Structural Homology, Protein
Protein Conformation, beta-Strand
Protein Multimerization
Carbohydrate Epimerases
Sequence Alignment
Homotetramer
Protein Binding
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Acta Crystallogr F Struct Biol Commun
- Accession number :
- edsair.doi.dedup.....11a518709829dfbc1f9907e7e0d74374