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Structure and function of PCD/DCoH, an enzyme with regulatory properties
Author(s) -
Suck Dietrich,
Ficner Ralf
Publication year - 1996
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(96)00573-x
Subject(s) - transcription factor , xenopus , coactivator , microbiology and biotechnology , binding site , function (biology) , biology , chemistry , biochemistry , enzyme , transcription (linguistics) , biophysics , gene , linguistics , philosophy
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.