2NRN

Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant

Summary for 2NRN

• Entry DOI: 10.2210/pdb2nrn/pdb
• Related: 2B1F 2B22 2HY6 2IPZ 2ZTA
• Descriptor: General control protein GCN4, PHOSPHATE ION (3 entities in total)
• Functional Keywords: coiled coils, tetramer, protein design, protein structure, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 4
• Total formula weight: 15990.31

Authors

Liu, J.,Lu, M. (deposition date: 2006-11-02, release date: 2007-04-17, Last modification date: 2023-08-30)

Primary citation

Deng, Y.,Zheng, Q.,Liu, J.,Cheng, C.S.,Kallenbach, N.R.,Lu, M.
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.
Protein Sci., 16:323-328, 2007

PubMed Abstract: The hydrophobic core of the GCN4 leucine-zipper dimerization domain is formed by a parallel helical association between nonpolar side chains at the a and d positions of the heptad repeat. Here we report a self-assembling coiled-coil array formed by the GCN4-pAe peptide that differs from the wild-type GCN4 leucine zipper by alanine substitutions at three charged e positions. GCN4-pAe is incompletely folded in normal solution conditions yet self-assembles into an antiparallel tetraplex in crystals by formation of unanticipated hydrophobic seams linking the last two heptads of two parallel double-stranded coiled coils. The GCN4-pAe tetramers in the lattice associate laterally through the identical interactions to those in the intramolecular dimer-dimer interface. The van der Waals packing interaction in the solid state controls extended supramolecular assembly of the protein, providing an unusual atomic scale view of a mesostructure.

PubMed: 17189475
DOI: 10.1110/ps.062590807

Experimental method

X-RAY DIFFRACTION (1.4 Å)