The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
The crystal structure of GMP synthetase serves as a prototype for two families of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP synthetase is found in related enzymes of the purine, pyrimidine, tryptophan, arginine, histidine and folic acid biosynthetic pathways. This domain includes a conserved Cys-His-Glu triad and is representative of a new family of enzymes that use a catalytic triad for enzymatic hydrolysis. The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase.
Tesmer
J J
JJ
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Klem
T J
TJ
Deras
M L
ML
Davisson
V J
VJ
Smith
J L
JL
D000595:Amino Acid Sequence; D019731:Carbon-Nitrogen Ligases; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D008025:Ligases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation
D008025:Ligases; D019731:Carbon-Nitrogen Ligases; C020828:GMP synthase (glutamine-hydrolyzing)