Literature summary for 2.7.7.B24 extracted from

Zhu, D.; Wang, L.; Shang, G.; Liu, X.; Zhu, J.; Lu, D.; Wang, L.; Kan, B.; Zhang, J.R.; Xiang, Y.
Structural biochemistry of a Vibrio cholerae dinucleotide cyclase reveals cyclase activity regulation by folates (2014), Mol. Cell., 55, 931-937.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Vibrio cholerae O1

Crystallization (Commentary)

Crystallization (Comment)	Organism
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 structures reveal 5-methyltetrahydrofolate diglutamate bound opposite the substrate-binding pocket	Vibrio cholerae O1

Crystallization (Comment)

Organism

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 structures reveal 5-methyltetrahydrofolate diglutamate bound opposite the substrate-binding pocket

Vibrio cholerae O1

Protein Variants

Protein Variants	Comment	Organism
D131A/D133A	crystallization data	Vibrio cholerae O1
D260A	residue involved in folate binding, protein cannort fold properly	Vibrio cholerae O1
F109P	residue involved in folate binding, enzyme activity is completely impaired	Vibrio cholerae O1
R108W	residue involved in folate binding, enzyme activity is completely impaired	Vibrio cholerae O1
R40A	residue involved in folate binding, enzyme activity is completely impaired	Vibrio cholerae O1
R44E	residue involved in folate binding, protein cannort fold properly	Vibrio cholerae O1
Y137R	residue involved in folate binding, enzyme activity is completely impaired	Vibrio cholerae O1

Inhibitors

Inhibitors	Comment	Organism
5-methyltetrahydrofolate di-glutamate	-	Vibrio cholerae O1
5-methyltetrahydrofolic acid	-	Vibrio cholerae O1
folic acid	-	Vibrio cholerae O1
tetrahydrofolic acid	-	Vibrio cholerae O1

Organism

Organism	UniProt	Comment	Textmining
Vibrio cholerae O1	Q9KVG7	-	-
Vibrio cholerae O1 ATCC 39315	Q9KVG7	-	-

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.00169	-	25°C, pH not specified in the publication	Vibrio cholerae O1	5-methyltetrahydrofolate di-glutamate
0.0339	-	25°C, pH not specified in the publication	Vibrio cholerae O1	5-methyltetrahydrofolic acid