Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia.
Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia.
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and 34 kDa ATP pyrophosphatase, ATPPase. Domain structure and interactions, structure-activity relationship of the functional subunits, overview
the glutamine amidotransferase GATase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of subunit ATP diphosphatase ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits
the glutamine amidotransferase GATase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of subunit ATP diphosphatase ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits
the glutamine amidotransferase GATase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of subunit ATP diphosphatase ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Maruoka, S.; Horita, S.; Lee, W.C.; Nagata, K.; Tanokura, M.
Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3