The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.


Abstract

The dimeric interface of the leucine zipper coiled coil from GCN4 has been used to probe the contributions of hydrophobic and hydrogen bonding interactions to protein stability. We have determined the energetics of placing Ile or Asn residues at four buried positions in a two-stranded coiled coil. As expected, Ile is favored over Asn at these buried positions, but not as much as predicted by considering only the hydrophobic effect. It appears that interstrand hydrogen bonds form between the side-chains of the buried Asn residues and these contribute to the conformational stability of the coiled-coil peptides. However, these contributions are highly dependent on the locations of the Asn pairs. The effect of an Ile to Asn mutation is greatest at the N terminus of the peptide and decreases almost twofold as we move the substitution from the N to C-terminal heptads. Study holds ProTherm entries: 8342, 8343, 8344, 8345, 8346, 8347, 8348, 8349, 8350, 8351, 8352, 8353, 8354, 8355, 8356, 8357 Extra Details: The variant of GCN4 at position 'a' is VNVV leucine zippers; protein stability; hydrogen bonds;,hydrophobic interaction

Submission Details

ID: KwUokZw64

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:36 p.m.

Version: 1

Publication Details
Zhu H;Celinski SA;Scholtz JM;Hu JC,J. Mol. Biol. (2000) The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil. PMID:10903875
Additional Information

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 PDB Entries

Structure ID Release Date Resolution Structure Title
1CE9 1999-03-18T00:00:00+0000 1.8 HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER
1DGC 1993-07-15T00:00:00+0000 3.0 THE X-RAY STRUCTURE OF THE GCN4-BZIP BOUND TO ATF/CREB SITE DNA SHOWS THE COMPLEX DEPENDS ON DNA FLEXIBILITY
1FAV 2000-07-13T00:00:00+0000 3.0 THE STRUCTURE OF AN HIV-1 SPECIFIC CELL ENTRY INHIBITOR IN COMPLEX WITH THE HIV-1 GP41 TRIMERIC CORE
1FMH 2000-08-17T00:00:00+0000 0 NMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER
1FMH 2000-08-17T00:00:00+0000 0 NMR SOLUTION STRUCTURE OF A DESIGNED HETERODIMERIC LEUCINE ZIPPER
1GCL 1993-10-20T00:00:00+0000 2.1 GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
1GCM 1995-04-25T00:00:00+0000 1.8 GCN4 LEUCINE ZIPPER CORE MUTANT P-LI
1GK6 2001-08-08T00:00:00+0000 1.9 Human vimentin coil 2B fragment linked to GCN4 leucine zipper (Z2B)
1GZL 2002-05-23T00:00:00+0000 1.8 Crystal structure of C14linkmid/IQN17: a cross-linked inhibitor of HIV-1 entry bound to the gp41 hydrophobic pocket
1IHQ 2001-04-19T00:00:00+0000 0 GLYTM1BZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF A RAT SHORT ALPHA TROPOMYOSIN WITH THE N-TERMINUS ENCODED BY EXON 1B

Relevant UniProtKB Entries

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