1ZII
GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE DIMERIC STATE
Summary for 1ZII
| Entry DOI | 10.2210/pdb1zii/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 | 2 |
| Total formula weight | 8005.41 |
| Authors | Gonzalez Junior, L.,Brown, R.A.,Richardson, D.,Alber, T. (deposition date: 1996-10-30, release date: 1997-07-07, Last modification date: 2024-06-05) |
| Primary citation | Gonzalez Junior, L.,Brown, R.A.,Richardson, D.,Alber, T. Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism Nat.Struct.Biol., 3:1002-1010, 1996 Cited by PubMed Abstract: Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement. PubMed: 8946853DOI: 10.1038/nsb1296-1002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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