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

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• 作者：Silvia Deiss¹ ; Birte Hernandez Alvarez¹ ; Kerstin Bä ; r ; Carolin P. Ewers ; Murray Coles ; Reinhard Albrecht ; Marcus D. Hartmann ; ^{marcus.hartmann@tuebingen.mpg.de" class="auth_mail}
• 关键词：Fusion protein ; Chimera ; Expression system
• 刊名：Journal of Structural Biology
• 出版年：June 2014
• 年：2014
• 卷：186
• 期：3
• 页码：380-385
• 全文大小：1128 K

文摘

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.