DNA recognition by GAL4: structure of a protein-DNA complex.
Marmorstein, R., Carey, M., Ptashne, M., Harrison, S.C.(1992) Nature 356: 408-414
- PubMed: 1557122 
- DOI: https://doi.org/10.1038/356408a0
- Primary Citation of Related Structures:  
1D66 - PubMed Abstract: 
A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.
- Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, Massachusetts.
Organizational Affiliation: