Crystallization and preliminary crystallographic studies of recombinant dimerization cofactor of transcription factor HNF1/pterin‐4α‐carbinolamine dehydratase from liver

FEBS Letters

Ceska, Thomas A.¹  Ficner, Ralf¹  Stier, Gunter¹  Sauer, Uwe H.¹  Suck, Dietrich¹ 

[1] EMBL, Structural Biology Programme, Meyerhofstrasse 1, 69117 Heidelberg, Germany

关键词: Transcription factor;    Phenylalanine hydroxylation;    Biopterin;    Crystallization;    X-ray crystallography;    CHES;    cyclohexylaminoethanesulfonic acid;    DCoH;    dimerization cofactor of HNF1;    DTT;    dithiothreitol;    EDTA;    ethylene diamine tetraacetic acid;    HNF;    hepatocyte nuclear factor;    IPTG;    isopropyl-β-d-thiogalactoside;    MES;    N-morpholinoethanesulfonic acid;    MPD;    methylpentanediol;    PCD;    Pterin-4α-carbinolamin dehydratase;   

DOI  :  10.1016/0014-5793(94)01325-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 P3₁21 (or P3₂21) with unit cell dimensions of . Native crystals diffract to a resolution of 2.5 Å.

【 授权许可】

Unknown