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|1d66, resolution 2.70Å ()|
DNA RECOGNITION BY GAL4: STRUCTURE OF A PROTEIN/DNA COMPLEX
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.
DNA recognition by GAL4: structure of a protein-DNA complex., Marmorstein R, Carey M, Ptashne M, Harrison SC, Nature. 1992 Apr 2;356(6368):408-14. PMID:1557122
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Hydrogen in macromolecular models
- User:Eric Martz/Introduction to Structural Bioinformatics I
- User:Eric Martz/Introduction to Structural Bioinformatics I%2C 2013
- User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions
- User:Wayne Decatur/Biochem642 Molecular Visualization Sessions
- User:Wayne Decatur/UNH BCHEM833 Structural Analysis Workshop Session Fall 2012