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4C46

ANDREI-N-LVPAS fused to GCN4 adaptors

Summary for 4C46
Entry DOI10.2210/pdb4c46/pdb
DescriptorGENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4, BROMIDE ION (3 entities in total)
Functional Keywordstranscription, ion coordination, polar core residues, fusion protein, chimera, coiled coil, proline
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
Total number of polymer chains3
Total formula weight26688.29
Authors
Primary citationDeiss, S.,Hernandez Alvarez, B.,Bar, K.,Ewers, C.P.,Coles, M.,Albrecht, R.,Hartmann, M.D.
Your Personalized Protein Structure: Andrei N. Lupas Fused to GCN4 Adaptors.
J.Struct.Biol., 186:380-, 2014
Cited by
PubMed 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.
PubMed: 24486584
DOI: 10.1016/J.JSB.2014.01.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2024-10-30公开中

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