1dch
From Proteopedia
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CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR
Overview
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.
About this Structure
1DCH is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator., Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T, Science. 1995 Apr 28;268(5210):556-9. PMID:7725101
Page seeded by OCA on Tue Nov 20 13:10:11 2007
