1GPM

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

1GPM の概要

• エントリーDOI: 10.2210/pdb1gpm/pdb
• 分子名称: GMP SYNTHETASE, PHOSPHATE ION, PYROPHOSPHATE 2-, ... (7 entities in total)
• 機能のキーワード: class i glutamine amidotransferase, n-type atp pyrophosphatase, transferase (glutamine amidotransferase)
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 238314.19

構造登録者

Tesmer, J.J.G. (登録日: 1995-04-04, 公開日: 1996-01-29, 最終更新日: 2024-02-07)

主引用文献

Tesmer, J.J.,Klem, T.J.,Deras, M.L.,Davisson, V.J.,Smith, J.L.
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Nat.Struct.Biol., 3:74-86, 1996

PubMed 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.

PubMed: 8548458
DOI: 10.1038/nsb0196-74

実験手法

X-RAY DIFFRACTION (2.2 Å)