The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

Nat Struct Biol. 1996 Jan;3(1):74-86. doi: 10.1038/nsb0196-74.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carbon-Nitrogen Ligases*
  • Conserved Sequence
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Ligases / chemistry*
  • Ligases / genetics
  • Molecular Sequence Data
  • Protein Conformation

Substances

  • Ligases
  • Carbon-Nitrogen Ligases
  • GMP synthase (glutamine-hydrolyzing)

Associated data

  • GENBANK/L25883
  • GENBANK/U00015