Summary information and primary citation
- PDB-id
-
1d66;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.7 Å)
- Summary
- DNA recognition by gal4: structure of a protein-DNA
complex
- Reference
-
Marmorstein R, Carey M, Ptashne M, Harrison SC (1992):
"DNA
recognition by GAL4: structure of a protein-DNA
complex." Nature, 356,
408-414. doi: 10.1038/356408a0.
- 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.
