The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex
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.
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In crystal structures of GCN4 homodimers and Jun-Fos heterodimers, g-e' intersubunit salt bridges are seen between oppositely charged residues at positions gi and e/+5.
“In the crystal structures of GCN4 homodimers and Jun-Fos heterodimers, g-e' intersubunit salt bridges are visible between oppositely charged amino acids in the gi and e/+5 positions (O'Shea et al., 1991; Ellenberger et al., 1992; Konig & Richmond, 1993; Glover & Harrison, 1995).”
From Oligomerization properties of GCN4 leucine zipper <i>e</i> and <i>g</i> position mutants (1997) · cites this paper as Ellenberger et al., 1992
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- Authors
- Ellenberger, T. E., Brandl, C. J., Struhl, K., & Harrison, S. C.
- Affiliations
- Harvard University (US)
- Howard Hughes Medical Institute (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1992-12
- Volume
- 71
- Issue
- 7
- Pages
- 1223-1237
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2039478144
- Cited by
- 972
- References
- 2
- Citations by year
- 2026: 12 · 2025: 11 · 2024: 10 · 2023: 21 · 2022: 17 · 2021: 26 · 2020: 13 · 2019: 14 · 2018: 23 · 2017: 14 · 2016: 21 · 2015: 32 · 2014: 24 · 2013: 25 · 2012: 29
- FWCI
- 26.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- Funders
- McKnight Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- GCN4, bZIP transcription factors, protein-DNA complex, coiled-coil dimerization, DNA-binding motifs, AP-1 binding site, protein-DNA contacts, crystal structure
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