Structure and function of PCD/DCoH, an enzyme with regulatory properties

FEBS Letters

Ficner, Ralf¹  Suck, Dietrich¹ 

[1] European Molecular Biology Laboratory, Structural Biology Programme, 69012 HeiDAlberg, Germany

关键词: Homeodomain;    Tetrahydrobiopterin;    Transcription activator;    X-ray structure;   

DOI  :  10.1016/0014-5793(96)00573-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The bifunctional protein PCD/DCoH is both an enzyme involved in the phenylalanine hydroxylation system and a transcription coactivator forming a 2:2 heterotetrameric complex with the nuclear transcription factor HNF1. The discovery of a bacterial homologue and the expression pattern during Xenopus embryogenesis suggest a regulatory function not only restricted to HNF1. The crystal structures of the tetrameric rat and the dimeric bacterial PCD/DCoH have led to the proposal of substrate and HNF1 binding sites. The saddle-shaped β-sheet surfaces of the DCoH dimers likely represent binding sites for as yet unknown macromolecular interaction partners. Possible mechanisms for DCoH-induced transcriptional regulation are discussed in the light of the three-dimensional structures.

【 授权许可】

Unknown