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Crystallization and preliminary crystallographic studies of recombinant dimerization cofactor of transcription factor HNF1/pterin‐4α‐carbinolamine dehydratase from liver
Author(s) -
Ficner Ralf,
Sauer Uwe H.,
Ceska Thomas A.,
Stier Gunter,
Suck Dietrich
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01325-u
Subject(s) - pterin , phenylalanine hydroxylase , cofactor , dehydratase , rhodanese , chemistry , biochemistry , biology , microbiology and biotechnology , enzyme , phenylalanine , amino acid
The bi‐functional protein dimerization cofactor of HNF1 (DCoH)/pterin‐4α‐carbinolamine dehydratase (PCD) is found in liver cell nuclei bound to the transcription factor hepatocyte nuclear factor 1 (HNF1) as well as in the cytoplasm acting as an enzyme involved in the phenylalanine hydroxylation system. Deficiency of DCoH/PCD activity in liver causes an atypical hyperphenylalaninemia and deficiency in human epidermis is related to the depigmentation disorder vitiligo. DCoH/PCD from rat liver, which is identical to the human protein, was expressed in E. coli , purified to homogeneity and crystallized. The crystals belong to the trigonal space group P3 1 21 (or P3 2 21) with unit cell dimensions of . Native crystals diffract to a resolution of 2.5 Å.