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6.3.5.2: GMP synthase (glutamine-hydrolysing)

This is an abbreviated version!
For detailed information about GMP synthase (glutamine-hydrolysing), go to the full flat file.

Word Map on EC 6.3.5.2

Reaction

ATP
+
XMP
 +
L-glutamine
 +
H2O
=
AMP
 +
diphosphate
 +
GMP
 +
L-glutamate

Synonyms

cgsA, di-GMP synthase A, EC 6.3.4.1, GATase, Glutamine amidotransferase, GMP synthase, GMP synthase [glutamine-hydrolyzing] subunit B, GMP synthetase, GMP synthetase (glutamine hydrolysing), GMPS, GUA, GuaA, Guanine monophosphate synthetase, Guanosine 5'-monophosphate synthetase, Guanosine 5-monophosphate synthetase, guanosine monophosphate synthetase, Guanosine monophosphate synthetase (glutamine-hydrolyzing), Guanylate synthetase, Guanylate synthetase (glutamine-hydrolyzing), More, PD0279, PH1346, Synthetase, guanylate, two-subunit-type GMP synthetase, Xanthosine 5'-phosphate amidotransferase, Xanthosine 5-monophosphate aminase, Xanthosine-5'-phosphate-ammonia ligase, Xanthosine-5'-phosphate:ammonia ligase (AMP-forming), Xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming), XMP aminase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
                6.3.5.2 GMP synthase (glutamine-hydrolysing)

Crystallization

Crystallization on EC 6.3.5.2 - GMP synthase (glutamine-hydrolysing)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.2 A resolution
-
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
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
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
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
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