1ZIM
GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE TRIMERIC STATE
Summary for 1ZIM
| Entry DOI | 10.2210/pdb1zim/pdb |
| Descriptor | GENERAL CONTROL PROTEIN GCN4 (2 entities in total) |
| Functional Keywords | leucine zipper, amino-acid biosynthesis, transcription regulation, activator, dna-binding, nuclear protein, coiled coil |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P03069 |
| Total number of polymer chains | 3 |
| Total formula weight | 12137.18 |
| Authors | Gonzalez Junior, L.,Woolfson, D.N.,Alber, T. (deposition date: 1996-10-30, release date: 1997-07-07, Last modification date: 2024-10-30) |
| Primary citation | Gonzalez Jr., L.,Woolfson, D.N.,Alber, T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nat.Struct.Biol., 3:1011-1018, 1996 Cited by PubMed Abstract: A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gln and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast, Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gln 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment. PubMed: 8946854DOI: 10.1038/nsb1296-1011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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