3GW0

UROD mutant G318R

Summary for 3GW0

• Entry DOI: 10.2210/pdb3gw0/pdb
• Related: 1uro
• Descriptor: Uroporphyrinogen decarboxylase (2 entities in total)
• Functional Keywords: uroporphyrinogen, decarboxylase, lyase, heme biosynthesis. porphyria, disease mutation, heme biosynthesis, phosphoprotein, porphyrin biosynthesis
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: P06132
• Total number of polymer chains: 1
• Total formula weight: 40931.91

Authors

Hill, C.P.,Phillips, J.D.,Whitby, F.G.,Warby, C.,Kushner, J.P. (deposition date: 2009-03-31, release date: 2009-07-07, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)