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

Yiqun Deng, Qi Zheng, Jie Liu, Chao Sheng Cheng, Neville R. Kallenbach, Min Lu

Research output: Contribution to journalArticlepeer-review

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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)323-328
Number of pages6
JournalProtein Science
Volume16
Issue number2
DOIs
StatePublished - Feb 2007

Keywords

  • Coiled-coil assembly
  • Protein engineering
  • Supramolecular structure

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Self-assembly of coiled-coil tetramers in the 1.40 A° structure of a leucine-zipper mutant'. Together they form a unique fingerprint.

Cite this