1SWI

GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A COMPLEXED WITH BENZENE

Summary for 1SWI

Entry DOI	10.2210/pdb1swi/pdb
Descriptor	GCN4P1, BENZENE (3 entities in total)
Functional Keywords	coiled coil, leucine zipper
Biological source	Saccharomyces cerevisiae (baker's yeast)
Total number of polymer chains	3
Total formula weight	11966.03
Authors	Gonzalez, L.,Plecs, J.,Alber, T. (deposition date: 1996-05-09, release date: 1996-11-08, Last modification date: 2024-02-14)
Primary citation	Gonzalez Jr., L.,Plecs, J.J.,Alber, T. An engineered allosteric switch in leucine-zipper oligomerization. Nat.Struct.Biol., 3:510-515, 1996 Cited by PubMed Abstract: Controversy remains about the role of core side-chain packing in specifying protein structure. To investigate the influence of core packing on the oligomeric structure of a coiled coil, we engineered a GCN4 leucine zipper mutant that switches from two to three strands upon binding the hydrophobic ligands cyclohexane and benzene. In solution these ligands increased the apparent thermal stability and the oligomerization order of the mutant leucine zipper. The crystal structure of the peptide-benzene complex shows a single benzene molecule bound at the engineered site in the core of the trimer. These results indicate that coiled coils are well-suited to function as molecular switches and emphasize that core packing is an important determinant of oligomerization specificity. PubMed: 8646536 DOI: 10.1038/nsb0696-510 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation