BRENDA - Enzyme Database

Structural biochemistry of a Vibrio cholerae dinucleotide cyclase reveals cyclase activity regulation by folates

Zhu, D.; Wang, L.; Shang, G.; Liu, X.; Zhu, J.; Lu, D.; Wang, L.; Kan, B.; Zhang, J.R.; Xiang, Y.; Mol. Cell. 55, 931-937 (2014)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
2.7.7.B24
expression in Escherichia coli
Vibrio cholerae O1
Crystallization (Commentary)
EC Number
Crystallization (Commentary)
Organism
2.7.7.B24
structures of wild-type and mutant D131A/D133A, both to 2.1 A resolution. Structure and topology are typical of the nucleotidyltransferase superfamily. The molecule has an elongated shape with a groove in the middle that separates the molecule into two distinct domains. The two catalytic aspartic acid residues (Asp131 and Asp133) are within a beta sheet that is located at the bottom wall of the substrate-binding groove of DncV. In complex with GTP, GTP1 is hydrogen bonded with one of the metal ions and the side chains of Ser114, Ser301, Lys287, Asp348, and Tyr117 at the inner wall of the groove. GTP2 is hydrogen bonded with the other bound metal ion and the side chains of Asp133, Asp193, and Asn112. Complex strucutures reveal 5-methyltetrahydrofolate diglutamate bound opposite the substrate-binding pocket
Vibrio cholerae O1
Engineering
EC Number
Protein Variants
Commentary
Organism
2.7.7.B24
D131A/D133A
crystallization data
Vibrio cholerae O1
2.7.7.B24
D260A
residue involved in folate binding, protein cannort fold properly
Vibrio cholerae O1
2.7.7.B24
F109P
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R108W
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R40A
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R44E
residue involved in folate binding, protein cannort fold properly
Vibrio cholerae O1
2.7.7.B24
Y137R
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
2.7.7.B24
5-methyltetrahydrofolate di-glutamate
-
Vibrio cholerae O1
2.7.7.B24
5-methyltetrahydrofolic acid
-
Vibrio cholerae O1
2.7.7.B24
folic acid
-
Vibrio cholerae O1
2.7.7.B24
tetrahydrofolic acid
-
Vibrio cholerae O1
Organism
EC Number
Organism
UniProt
Commentary
Textmining
2.7.7.B24
Vibrio cholerae O1
Q9KVG7
-
-
2.7.7.B24
Vibrio cholerae O1 ATCC 39315
Q9KVG7
-
-
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
2.7.7.B24
0.00169
-
25°C, pH not specified in the publication
Vibrio cholerae O1
5-methyltetrahydrofolate di-glutamate
2.7.7.B24
0.0339
-
25°C, pH not specified in the publication
Vibrio cholerae O1
5-methyltetrahydrofolic acid
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.7.7.B24
expression in Escherichia coli
Vibrio cholerae O1
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.7.7.B24
structures of wild-type and mutant D131A/D133A, both to 2.1 A resolution. Structure and topology are typical of the nucleotidyltransferase superfamily. The molecule has an elongated shape with a groove in the middle that separates the molecule into two distinct domains. The two catalytic aspartic acid residues (Asp131 and Asp133) are within a beta sheet that is located at the bottom wall of the substrate-binding groove of DncV. In complex with GTP, GTP1 is hydrogen bonded with one of the metal ions and the side chains of Ser114, Ser301, Lys287, Asp348, and Tyr117 at the inner wall of the groove. GTP2 is hydrogen bonded with the other bound metal ion and the side chains of Asp133, Asp193, and Asn112. Complex strucutures reveal 5-methyltetrahydrofolate diglutamate bound opposite the substrate-binding pocket
Vibrio cholerae O1
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
2.7.7.B24
D131A/D133A
crystallization data
Vibrio cholerae O1
2.7.7.B24
D260A
residue involved in folate binding, protein cannort fold properly
Vibrio cholerae O1
2.7.7.B24
F109P
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R108W
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R40A
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
2.7.7.B24
R44E
residue involved in folate binding, protein cannort fold properly
Vibrio cholerae O1
2.7.7.B24
Y137R
residue involved in folate binding, enzyme activity is completely impaired
Vibrio cholerae O1
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
2.7.7.B24
0.00169
-
25°C, pH not specified in the publication
Vibrio cholerae O1
5-methyltetrahydrofolate di-glutamate
2.7.7.B24
0.0339
-
25°C, pH not specified in the publication
Vibrio cholerae O1
5-methyltetrahydrofolic acid
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
2.7.7.B24
5-methyltetrahydrofolate di-glutamate
-
Vibrio cholerae O1
2.7.7.B24
5-methyltetrahydrofolic acid
-
Vibrio cholerae O1
2.7.7.B24
folic acid
-
Vibrio cholerae O1
2.7.7.B24
tetrahydrofolic acid
-
Vibrio cholerae O1