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Self‐assembly of coiled‐coil tetramers in the 1.40 Å structure of a leucine‐zipper mutant
Author(s) -
Deng Yiqun,
Zheng Qi,
Liu Jie,
Cheng ChaoSheng,
Kallenbach Neville R.,
Lu Min
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062590807
Subject(s) - leucine zipper , coiled coil , dimer , crystallography , zipper , heptad repeat , antiparallel (mathematics) , chemistry , van der waals force , intramolecular force , supramolecular chemistry , basic helix loop helix leucine zipper transcription factors , monomer , bzip domain , biophysics , stereochemistry , peptide sequence , molecule , crystal structure , transcription factor , biochemistry , dna binding protein , biology , polymer , quantum mechanics , magnetic field , physics , organic chemistry , gene , algorithm , computer science
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.