2ZTA

X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL

Summary for 2ZTA

• Entry DOI: 10.2210/pdb2zta/pdb
• Descriptor: GCN4 LEUCINE ZIPPER (2 entities in total)
• Functional Keywords: leucine zipper
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 2
• Total formula weight: 8063.40

Authors

O'Shea, E.K.,Klemm, J.D.,Kim, P.S.,Alber, T. (deposition date: 1991-07-05, release date: 1992-10-15, Last modification date: 2024-10-09)

Primary citation

O'Shea, E.K.,Klemm, J.D.,Kim, P.S.,Alber, T.
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.
Science, 254:539-544, 1991

PubMed Abstract: The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of alpha helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.

PubMed: 1948029

Experimental method

X-RAY DIFFRACTION (1.8 Å)