2nrn
From Proteopedia
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Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant
Overview
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.
About this Structure
2NRN is a Single protein structure of sequence from Saccharomyces cerevisiae with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant., Deng Y, Zheng Q, Liu J, Cheng CS, Kallenbach NR, Lu M, Protein Sci. 2007 Feb;16(2):323-8. Epub 2006 Dec 22. PMID:17189475
Page seeded by OCA on Wed Nov 21 12:52:07 2007
