1YSA

THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA HELICES: CRYSTAL STRUCTURE OF THE PROTEIN-DNA COMPLEX

Summary for 1YSA

• Entry DOI: 10.2210/pdb1ysa/pdb
• Descriptor: DNA (5'-D(*TP*TP*CP*CP*TP*AP*TP*GP*AP*CP*TP*CP*AP*TP*CP*CP*A P*GP*TP*T)-3'), DNA (5'-D(*AP*AP*AP*CP*TP*GP*GP*AP*TP*GP*AP*GP*TP*CP*AP*TP*A P*GP*GP*A)-3'), PROTEIN (GCN4), ... (4 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: 4
• Total formula weight: 26050.13

Authors

Ellenberger, T.E.,Brandl, C.J.,Struhl, K.,Harrison, S.C. (deposition date: 1993-08-09, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Ellenberger, T.E.,Brandl, C.J.,Struhl, K.,Harrison, S.C.
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex.
Cell(Cambridge,Mass.), 71:1223-1237, 1992

PubMed Abstract: The yeast transcriptional activator GCN4 is 1 of over 30 identified eukaryotic proteins containing the basic region leucine zipper (bZIP) DNA-binding motif. We have determined the crystal structure of the GCN4 bZIP element complexed with DNA at 2.9 A resolution. The bZIP dimer is a pair of continuous alpha helices that form a parallel coiled coil over their carboxy-terminal 30 residues and gradually diverge toward their amino termini to pass through the major groove of the DNA-binding site. The coiled-coil dimerization interface is oriented almost perpendicular to the DNA axis, giving the complex the appearance of the letter T. There are no kinks or sharp bends in either bZIP monomer. Numerous contacts to DNA bases and phosphate oxygens are made by basic region residues that are conserved in the bZIP protein family. The details of the bZIP dimer interaction with DNA can explain recognition of the AP-1 site by the GCN4 protein.

PubMed: 1473154
DOI: 10.1016/S0092-8674(05)80070-4

Experimental method

X-RAY DIFFRACTION (2.9 Å)