EC Number   |
|---|
    6.3.5.2 | - |
| 6.3.5.2 | at 2.2 A resolution |
| 6.3.5.2 | ATPPase subunit of the two-subunit-type GMPS, sitting drop vapor diffusion at 5°C, mixing of 0.001 ml of protein solution containing 30 mg/ml protein in Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 30% v/v PEG 400, 100 mM Tris-HCl, pH 8.4, and 200 mM MgCl2, equilibration against 0.1 ml of reservoir solution, 3 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution |
| 6.3.5.2 | crystal structure of the ATPPase subunit of the two-subunit-type GMPS, to 1.79 A resolution. ATPPase consists of a N-domain and a C-domain and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate-binding site and also contributes to homodimerization. The glutamine amidotransferase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of PH-ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits |
| 6.3.5.2 | hanging-drop vapor-diffusion method at 5°C, crystal structure is determined at 1.89 A resolution. Its overall structure and active site are the most similar to those of Escherichia coli guanosine 5'-monophosphate synthase and Sulfolobus solfataricus anthranilate synthase, respectively |
| 6.3.5.2 | in complex with XMP, sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate, pH 5.2, 1.6 M ammonium sulfate, and 0.2 M sodium chloride, at 25°C |
| 6.3.5.2 | structural model of GMPS in a closed, active state. The salt bridge between residues H186 and E383 functions as a connection between the two active sites |
