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

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

Author information

1
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany.
2
Department of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstraße 35, D-72076 Tübingen, Germany. Electronic address: marcus.hartmann@tuebingen.mpg.de.

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

PMID:
24486584
DOI:
10.1016/j.jsb.2014.01.013
[Indexed for MEDLINE]
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