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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.B24 expression in Escherichia coli Vibrio cholerae O1

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment 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 Comment 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 Comment 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 Comment 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