2ATF

X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056

2ATF の概要

• エントリーDOI: 10.2210/pdb2atf/pdb
• 分子名称: Cysteine dioxygenase type I, NICKEL (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: mm.241056, pfam05995.2 cdo_i, bc013638, cupin family, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, oxidoreductase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23276.22

構造登録者

Wesenberg, G.E.,Phillips Jr., G.N.,Mccoy, J.G.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2005-08-24, 公開日: 2005-10-18, 最終更新日: 2024-10-30)

主引用文献

McCoy, J.G.,Bailey, L.J.,Bitto, E.,Bingman, C.A.,Aceti, D.J.,Fox, B.G.,Phillips, G.N.
Structure and mechanism of mouse cysteine dioxygenase.
Proc.Natl.Acad.Sci.Usa, 103:3084-3089, 2006

PubMed Abstract: Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme.

PubMed: 16492780
DOI: 10.1073/pnas.0509262103

実験手法

X-RAY DIFFRACTION (1.75 Å)