1PSD

THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE

1PSD の概要

• エントリーDOI: 10.2210/pdb1psd/pdb
• 分子名称: D-3-PHOSPHOGLYCERATE DEHYDROGENASE (PHOSPHOGLYCERATE DEHYDROGENASE), NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SERINE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase (nad(a))
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89727.90

構造登録者

Schuller, D.J.,Grant, G.A.,Banaszak, L.J. (登録日: 1995-05-02, 公開日: 1995-07-31, 最終更新日: 2024-02-14)

主引用文献

Schuller, D.J.,Grant, G.A.,Banaszak, L.J.
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
Nat.Struct.Biol., 2:69-76, 1995

PubMed Abstract: The crystal structure of the phosphoglycerate dehydrogenase from Escherichia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. The tetramer has approximate 222 symmetry with the principal contacts between the subunits forming between either the nucleotide binding domains or the regulatory domains. Two slightly different subunit conformations are present which vary only in the orientations of the domains. There is a hinge-like arrangement near the active site cleft and the serine effector site is provided by the regulatory domain of each of two subunits. Interdomain flexibility may play a key role in both catalysis and allosteric inhibition.

PubMed: 7719856
DOI: 10.1038/nsb0195-69

実験手法

X-RAY DIFFRACTION (2.75 Å)