1GCM
GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
Summary for 1GCM
| Entry DOI | 10.2210/pdb1gcm/pdb |
| Descriptor | GCN4P-II (2 entities in total) |
| Functional Keywords | hydrophobic core mutant, transcription regulation |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P03069 |
| Total number of polymer chains | 3 |
| Total formula weight | 12218.51 |
| Authors | Harbury, P.B.,Kim, P.S.,Alber, T. (deposition date: 1995-04-25, release date: 1996-01-29, Last modification date: 2021-11-03) |
| Primary citation | Harbury, P.B.,Kim, P.S.,Alber, T. Crystal structure of an isoleucine-zipper trimer. Nature, 371:80-83, 1994 Cited by PubMed Abstract: Subunit oligomerization in many proteins is mediated by short coiled-coil motifs. These motifs share a characteristic seven-amino-acid repeat containing hydrophobic residues at the first (a) and fourth (d) positions. Despite this common pattern, different sequences form two-, three- and four-stranded helical ropes. We have investigated the basis for oligomer choice by characterizing variants of the GCN4 leucine-zipper dimerization domain that adopt trimeric or tetrameric structures in response to mutations at the a and d positions. We now report the high-resolution X-ray crystal structure of an isoleucine-containing mutant that folds into a parallel three-stranded, alpha-helical coiled coil. In contrast to the dimer and tetramer structures, the interior packing of the trimer can accommodate beta-branched residues in the most preferred rotamer at both hydrophobic positions. Compatibility of the shape of the core amino acids with the distinct packing spaces in the two-, three- and four-stranded conformations appears to determine the oligomerization state of the GCN4 leucine-zipper variants. PubMed: 8072533DOI: 10.1038/371080a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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