EC Number   |
|---|
  2.7.7.B24 | structure in complex with dGTP. DncV adopts an extended bilobed architecture characterized by a nucleotidyltransferase fold |
| 2.7.7.B24 | structure of apo form and in complex with GTP and with dATP and dGTP, respectively. DncV adopts an extended bilobed architecture characterized by a nucleotidyltransferase fold. The ribose and triphosphate moieties of both GTP and ATP are bound to the donor and acceptor pockets in a similar manner. DncV efficiently catalyzes the phosphodiester linkage formation with ATP bound to the acceptor pocket, compared with GTP, thereby producing pppA(3'5')pG preferentially |
| 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 |
| 2.7.7.B24 | wild-type and mutant D131N/D133N. Catalytic residues are D131 and D133 in strand beta1, and D193 in strand beta5, and the G[G/S]xx motif is defined by residues G113-S114-F115-Q116 in a well-defined loop linking helix alpha5 and strand beta1 |
