TY - JOUR
T1 - The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices
T2 - Crystal structure of the protein-DNA complex
AU - Ellenberger, Thomas E.
AU - Brandl, Christopher J.
AU - Struhl, Kevin
AU - Harrison, Stephen C.
N1 - Funding Information:
We thank Drs. Tom Alber and Erin O'Shea for providing coordinates of the GCN4 leuoine zipper peptide prior to publication and members of the Harrison and Struht laboratories for discussions and suggestions. This work was funded in part by National Institutes of Health grants to S. C. H. and to K. S. and by the Lucille P. Markey Charitable Trust. C. J. B. was supported by a fellowship from the Medical Research Council of Canada. T. E. E. is a Luoille P. Markey Scholar. Coordinates of the GCN4 complex are being deposited in the Brookha-ven Data Bank.
PY - 1992/12/24
Y1 - 1992/12/24
N2 - 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 Å resolution. The bZIP dimer is a pair of continuous α 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.
AB - 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 Å resolution. The bZIP dimer is a pair of continuous α 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.
UR - https://www.scopus.com/pages/publications/0027049805
U2 - 10.1016/S0092-8674(05)80070-4
DO - 10.1016/S0092-8674(05)80070-4
M3 - Article
C2 - 1473154
AN - SCOPUS:0027049805
SN - 0092-8674
VL - 71
SP - 1223
EP - 1237
JO - Cell
JF - Cell
IS - 7
ER -