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Structure and function of PCD/DCoH, an enzyme with regulatory properties
1European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, Germany.
FEBS Letters
|June 24, 1996
Summary
The bifunctional enzyme Phenylalanine hydroxylase (PAH)/DCoH acts as a transcription coactivator for HNF1. Its structure suggests broader regulatory roles beyond HNF1, potentially involving other macromolecular partners.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- The protein PCD/DCoH possesses dual functions: enzymatic activity in phenylalanine metabolism and transcriptional coactivation.
- It forms a heterotetrameric complex with the transcription factor HNF1, indicating a role in gene regulation.
Purpose of the Study:
- To investigate the broader regulatory functions of PCD/DCoH beyond its interaction with HNF1.
- To elucidate the structural basis for PCD/DCoH's interactions and functions.
Main Methods:
- Analysis of crystal structures of rat (tetrameric) and bacterial (dimeric) PCD/DCoH.
- Comparative analysis of homologous structures.
Main Results:
- Proposed substrate and HNF1 binding sites based on crystal structures.
- Identified saddle-shaped beta-sheet surfaces on DCoH dimers as potential interaction sites for unknown partners.
- Expression patterns in Xenopus embryogenesis suggest roles beyond HNF1 regulation.
Conclusions:
- PCD/DCoH's structural features suggest a regulatory role extending to interactions with unidentified macromolecular partners.
- Structural insights provide a basis for understanding DCoH-mediated transcriptional regulation mechanisms.