An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper.


We previously reported that a helical trigger segment within the GCN4 leucine zipper monomer is indispensable for the formation of its parallel two-stranded coiled coil. Here, we demonstrate that the intrinsic secondary structure of the trigger site is largely stabilized by an intrahelical salt bridge. Removal of this surface salt bridge by a single amino acid mutation induced only minor changes in the backbone structure of the GCN4 leucine zipper dimer as verified by nuclear magnetic resonance. The mutation, however, substantially destabilized the dimeric structure. These findings support the proposed hierarchic folding mechanism of the GCN4 coiled coil in which local helix formation within the trigger segment precedes dimerization. Study holds ProTherm entries: 10821, 10822, 10823, 10824 Extra Details: helical trigger segment; two-stranded coiled coil; surface salt bridge;,dimeric structure; hierarchic folding mechanism; local helix formation

Submission Details

ID: zv7xz4b63

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Kammerer RA;Jaravine VA;Frank S;Schulthess T;Landwehr R;Lustig A;Garcia-Echeverria C;Alexandrescu AT;Engel J;Steinmetz MO,J. Biol. Chem. (2001) An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper. PMID:11134036
Additional Information

Study Summary

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 General control protein GCN4 P03069 GCN4_YEAST