1DCH

CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR

Summary for 1DCH

• Entry DOI: 10.2210/pdb1dch/pdb
• Descriptor: DCOH (DIMERIZATION COFACTOR OF HNF-1), SULFATE ION (2 entities in total)
• Functional Keywords: transcriptional simulator, dimerization cofactor, dehydratase, 4a-carbinolamine dehydratase, transregulator of homeodomain proteins, transcriptional stimulator, dimerization
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 8
• Total formula weight: 96909.33

Authors

Endrizzi, J.A.,Cronk, J.D.,Wang, W.,Crabtree, G.R.,Alber, T. (deposition date: 1995-01-24, release date: 1996-03-08, Last modification date: 2024-02-07)

Primary citation

Endrizzi, J.A.,Cronk, J.D.,Wang, W.,Crabtree, G.R.,Alber, T.
Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator.
Science, 268:556-559, 1995

PubMed Abstract: DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids.

PubMed: 7725101

Experimental method

X-RAY DIFFRACTION (3 Å)