2zta
From Proteopedia
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| , resolution 1.8Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF THE GCN4 LEUCINE ZIPPER, A TWO-STRANDED, PARALLEL COILED COIL
Overview
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.
About this Structure
2ZTA is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 2ZTA with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil., O'Shea EK, Klemm JD, Kim PS, Alber T, Science. 1991 Oct 25;254(5031):539-44. PMID:1948029
Page seeded by OCA on Mon Mar 31 05:21:02 2008
