3GW3

human UROD mutant K297N

3GW3 の概要

• エントリーDOI: 10.2210/pdb3gw3/pdb
• 関連するPDBエントリー: 1uro
• 分子名称: Uroporphyrinogen decarboxylase (2 entities in total)
• 機能のキーワード: uroporphyrinogen, decarboxylase, lyase, heme biosynthesis, porphyria, disease mutation, phosphoprotein, porphyrin biosynthesis
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: P06132
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40816.69

構造登録者

Hill, C.P.,Phillips, J.D.,Whitby, F.G.,Warby, C.,Kushner, J.P. (登録日: 2009-03-31, 公開日: 2009-07-07, 最終更新日: 2024-02-21)

主引用文献

Warby, C.A.,Phillips, J.D.,Bergonia, H.A.,Whitby, F.G.,Hill, C.P.,Kushner, J.P.
Structural and kinetic characterization of mutant human uroporphyrinogen decarboxylases.
Cell Mol Biol (Noisy-le-grand), 55:40-45, 2009

PubMed Abstract: Porphyria cutanea tarda (PCT) is caused by inhibition of uroporphyrinogen decarboxylase (URO-D) activity in hepatocytes. Subnormal URO-D activity results in accumulation and urinary excretion of uroporphyrin and heptacarboxyl porphyrin. Heterozygosity for mutations in the URO-D gene is found in the familial form of PCT (F-PCT). Over 70 mutations of URO-D have been described but very few have been characterized structurally. Here we characterize 3 mutations in the URO-D gene found in patients with F-PCT, G318R, K297N, and D306Y. Expression of the D306Y mutation results in an insoluble recombinant protein. G318R and K297N have little effect on the structure or activity of recombinant URO-D, but the proteins display reduced stability in vitro.

PubMed: 19656450

実験手法

X-RAY DIFFRACTION (1.7 Å)