1D66
DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX
Summary for 1D66
Entry DOI | 10.2210/pdb1d66/pdb |
Descriptor | DNA (5'-D(*CP*CP*GP*GP*AP*GP*GP*AP*CP*AP*GP*TP*CP*CP*TP*CP*C P*GP*G)-3'), DNA (5'-D(*CP*CP*GP*GP*AP*GP*GP*AP*CP*TP*GP*TP*CP*CP*TP*CP*C P*GP*G)-3'), PROTEIN (GAL4), ... (5 entities in total) |
Functional Keywords | protein-dna complex, double helix, transcription-dna complex, transcription/dna |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Nucleus: P04386 |
Total number of polymer chains | 4 |
Total formula weight | 27736.86 |
Authors | Marmorstein, R.,Carey, M.,Ptashne, M.,Harrison, S.C. (deposition date: 1992-03-06, release date: 1992-03-06, Last modification date: 2024-02-07) |
Primary citation | Marmorstein, R.,Carey, M.,Ptashne, M.,Harrison, S.C. DNA recognition by GAL4: structure of a protein-DNA complex. Nature, 356:408-414, 1992 Cited by 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. PubMed: 1557122DOI: 10.1038/356408a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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