1YSA

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

1YSA の概要

• エントリーDOI: 10.2210/pdb1ysa/pdb
• 分子名称: 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)
• 機能のキーワード: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P03069
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 26050.13

構造登録者

Ellenberger, T.E.,Brandl, C.J.,Struhl, K.,Harrison, S.C. (登録日: 1993-08-09, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)