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
This work presents a protein structure that has been designed purely for aesthetic reasons, symbolizing decades of coiled-coil research and praising its most fundamental model system, the GCN4 leucine zipper. The GCN4 leucine zipper is a highly stable coiled coil which can be tuned to adopt different oligomeric states via mutation of its core residues. For these reasons it is used in structural studies as a stabilizing fusion adaptor. On the occasion of the 50th birthday of Andrei N. Lupas, we used it to create the first personalized protein structure: we fused the sequence ANDREI-N-LVPAS in heptad register to trimeric GCN4 adaptors and determined its structure by X-ray crystallography. The structure demonstrates the robustness and versatility of GCN4 as a fusion adaptor. We learn how proline can be accommodated in trimeric coiled coils, and put the structure into the context of the other GCN4-fusion structures known to date.
Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors.,Deiss S, Hernandez Alvarez B, Bar K, Ewers CP, Coles M, Albrecht R, Hartmann MD J Struct Biol. 2014 Jan 29. pii: S1047-8477(14)00024-0. doi:, 10.1016/j.jsb.2014.01.013. PMID:24486584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deiss S, Hernandez Alvarez B, Bar K, Ewers CP, Coles M, Albrecht R, Hartmann MD. Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors. J Struct Biol. 2014 Jan 29. pii: S1047-8477(14)00024-0. doi:, 10.1016/j.jsb.2014.01.013. PMID:24486584 doi:https://dx.doi.org/10.1016/j.jsb.2014.01.013
