1DGC

THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF/CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY

Summary for 1DGC

• Entry DOI: 10.2210/pdb1dgc/pdb
• Descriptor: DNA (5'-D(*TP*GP*GP*AP*GP*AP*TP*GP*AP*CP*GP*TP*CP*AP*TP*CP*T P*CP*C)-3'), PROTEIN (GCN4) (2 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 2
• Total formula weight: 13065.14

Authors

Koenig, P.,Richmond, T.J. (deposition date: 1993-07-15, release date: 1994-06-22, Last modification date: 2024-02-07)

Primary citation

Konig, P.,Richmond, T.J.
The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility.
J.Mol.Biol., 233:139-154, 1993

PubMed Abstract: The X-ray structure of the DNA binding domain of the yeast transcriptional activator protein GCN4 bound to a DNA fragment containing the sequence of the perfectly symmetrical ATF/CREB site has been solved to 3.0 A resolution. The architecture of this specific recognition complex supports the current model for bZIP proteins: a homodimer of parallel alpha-helices form an interhelix coiled-coil region via the leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. The structure shows that DNA flexibility plays the predominant role in the preservation of protein contacts with the symmetric ATF/CREB site (ATGACGTCAT) as compared to the pseudo-symmetric AP-1 target site (ATGACTCAT), overcoming the positional displacement of functional groups introduced by the additional G.C base-pair at the center of the ATF/CREB sequence.

PubMed: 8377181
DOI: 10.1006/jmbi.1993.1490

Experimental method

X-RAY DIFFRACTION (3 Å)