3ICD

STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE

3ICD の概要

• エントリーDOI: 10.2210/pdb3icd/pdb
• 分子名称: ISOCITRATE DEHYDROGENASE (2 entities in total)
• 機能のキーワード: oxidoreductase (nad(a)-choh(d))
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45809.56

構造登録者

Hurley, J.H.,Thorsness, P.E.,Ramalingam, V.,Helmers, N.H.,Koshlandjunior, D.E.,Stroud, R.M. (登録日: 1989-12-28, 公開日: 1991-01-15, 最終更新日: 2024-02-21)

主引用文献

Hurley, J.H.,Thorsness, P.E.,Ramalingam, V.,Helmers, N.H.,Koshland Jr., D.E.,Stroud, R.M.
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
Proc.Natl.Acad.Sci.USA, 86:8635-8639, 1989

PubMed Abstract: The structure of isocitrate dehydrogenase [threo-DS-isocitrate: NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42] from Escherichia coli has been solved and refined at 2.5 A resolution and is topologically different from that of any other dehydrogenase. This enzyme, a dimer of identical 416-residue subunits, is inactivated by phosphorylation at Ser-113, which lies at the edge of an interdomain pocket that also contains many residues conserved between isocitrate dehydrogenase and isopropylmalate dehydrogenase. Isocitrate dehydrogenase contains an unusual clasp-like domain in which both polypeptide chains in the dimer interlock. Based on the structure of isocitrate dehydrogenase and conservation with isopropylmalate dehydrogenase, we suggest that the active site lies in an interdomain pocket close to the phosphorylation site.

PubMed: 2682654
DOI: 10.1073/pnas.86.22.8635

実験手法

X-RAY DIFFRACTION (2.5 Å)