Self-Assembly of Coiled-coil Tetramers in the 1.40 A Structure of a Leucine-zipper Mutant

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Protein Science

OSTI ID:929879

Deng, Y; Zheng, Q; Liu, J; Cheng, C; Kallenbach, N; Lu, M

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 doublestranded 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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 929879
• Report Number(s): BNL--80451-2008-JA
• Journal Information: Protein Science, Journal Name: Protein Science Vol. 16
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ALANINES
CRYSTALS
DIMERIZATION
INTERACTIONS
LEUCINE
MUTANTS
PEPTIDES
SOLIDS
SOLUTIONS
national synchrotron light source