3D3W

Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.

3D3W の概要

• エントリーDOI: 10.2210/pdb3d3w/pdb
• 関連するPDBエントリー: 1PR9
• 分子名称: L-xylulose reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: l-xylulose reductase, uronate cycle, short-chain dehydrogenase/reductase(sdr) superfamily, glucose metabolism, acetylation, carbohydrate metabolism, membrane, nadp, oxidoreductase, xylose metabolism
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Membrane; Peripheral membrane protein (By similarity): Q7Z4W1 Q7Z4W1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53479.85

構造登録者

Zhao, H.-T.,El-Kabbani, O. (登録日: 2008-05-12, 公開日: 2009-04-21, 最終更新日: 2024-11-13)

主引用文献

Zhao, H.T.,Endo, S.,Ishikura, S.,Chung, R.,Hogg, P.J.,Hara, A.,El-Kabbani, O.
Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase.
Cell.Mol.Life Sci., 66:1570-1579, 2009

PubMed Abstract: L-xylulose reductase (XR) is involved in water re-absorption and cellular osmoregulation. The crystal structure of human XR complemented with site-directed mutagenesis (Cys138Ala) indicated that the disulfide bond in the active site between Cys138 and Cys150 is unstable and may affect the reactivity of the enzyme. The effects of reducing agents on the activities of the wild-type and mutant enzymes indicated the reversibility of disulfide-bond formation, which resulted in three-fold decrease in catalytic efficiency. Furthermore, the addition of cysteine (>2 mM) inactivated human XR and was accompanied by a 10-fold decrease in catalytic efficiency. TOF-MS analysis of the inactivated enzyme showed the S-cysteinylation of Cys138 in the wild-type and Cys150 in the mutant enzymes. Thus, the action of human XR may be regulated by cellular redox conditions through reversible disulfide-bond formation and by S-cysteinylation.

PubMed: 19337691
DOI: 10.1007/s00018-009-9065-y

実験手法

X-RAY DIFFRACTION (1.87 Å)