Structural highlights
Function
GCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
Publication Abstract from PubMed
The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-type GCN4 leucine zipper by alanine substitutions at three charged e positions. GCN4-pAe is incompletely folded in normal solution conditions yet self-assembles into an antiparallel tetraplex in crystals by formation of unanticipated hydrophobic seams linking the last two heptads of two parallel double-stranded coiled coils. The GCN4-pAe tetramers in the lattice associate laterally through the identical interactions to those in the intramolecular dimer-dimer interface. The van der Waals packing interaction in the solid state controls extended supramolecular assembly of the protein, providing an unusual atomic scale view of a mesostructure.
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.,Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M Protein Sci. 2007 Feb;16(2):323-8. Epub 2006 Dec 22. PMID:17189475[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M. Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant. Protein Sci. 2007 Feb;16(2):323-8. Epub 2006 Dec 22. PMID:17189475 doi:ps.062590807
