Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors

J Struct Biol. 2014 Jun;186(3):380-5. doi: 10.1016/j.jsb.2014.01.013. Epub 2014 Jan 29.

Abstract

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.

Keywords: Chimera; Expression system; Fusion protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Basic-Leucine Zipper Transcription Factors / chemistry*
  • Basic-Leucine Zipper Transcription Factors / metabolism
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Proline
  • Protein Engineering / methods*
  • Protein Structure, Secondary
  • Recombinant Fusion Proteins / chemistry*
  • Recombinant Fusion Proteins / metabolism
  • Repetitive Sequences, Amino Acid
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • Basic-Leucine Zipper Transcription Factors
  • GCN4 protein, S cerevisiae
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Proline

Associated data

  • PDB/4C46