Summary information and primary citation

PDB-id
1d66; SNAP-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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js