PDBsum entry 1dch

Transcriptional stimulator,dimerization

PDB id: 1dch

Contents

Protein chains

(+ 2 more) 99 a.a. *

Ligands

SO4 ×8

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: Crystal structure of dcoh, A bifunctional, Protein-Binding transcriptional coactivator.
• Authors: J.A.Endrizzi, J.D.Cronk, W.Wang, G.R.Crabtree, T.Alber.
• Ref.: Science, 1995, 268, 556-559. [DOI no: 10.1126/science.7725101]
• PubMed id: 7725101

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.