Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors.
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.
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Silvia
S
Deiss
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Birte
B
Hernandez Alvarez
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Kerstin
K
Bär
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Carolin P
CP
Ewers
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Murray
M
Coles
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
Reinhard
R
Albrecht
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany. Electronic address: marcus.hartmann@tuebingen.mpg.de.
Marcus D
MD
Hartmann
D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011392:Proline; D015202:Protein Engineering / Q000379:methods*; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000378:metabolism; D020449:Repetitive Sequences, Amino Acid; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
D050976:Basic-Leucine Zipper Transcription Factors; C501391:GCN4 protein, S cerevisiae; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D011392:Proline
Chimera; Expression system; Fusion protein