Beasley met sandbox
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 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.
| |||||||||
| 1d66, resolution 2.70Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | |||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEXDNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX
About this StructureAbout this Structure
1d66 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Marmorstein R, Carey M, Ptashne M, Harrison SC. DNA recognition by GAL4: structure of a protein-DNA complex. Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122 doi:http://dx.doi.org/10.1038/356408a0