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

被引：22

作者：

Suck, D ^{[1
]}

Ficner, R ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,STRUCT BIOL PROGRAMME,D-69012 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1996年 / 389卷 / 01期

关键词：

homeodomain; tetrahydrobiopterin; transcription activator; X-ray structure;

D O I：

10.1016/0014-5793(96)00573-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 beta-sheet surfaces of the DCoH diners 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.

引用

页码：35 / 39

页数：5