The resonance assignment, secondary structure, and dynamic properties of a stable noncoiled coil conformation of the dimerization domain from yeast transcription activation factor GCN4 (Leu zipper; LZGCN4) are presented. Introduced in this paper, a new line of fully optimized spin state exchange experiments, XYEX-TROSY, applied to 1HN, 15N and 1Halpha,13Calpha moieties, established that in broad range of pH and buffer conditions the classical LZGCN4 coiled coil dimer is in a dynamic equilibrium with another distinct conformation (denoted here as x-form) and enabled complete assignment of the resonances stemming from the x-form. The LZGCN4 x-form is generally less structured in comparison with the classical GCN4-p1 coiled coil, but still retains a structured alpha-helical central core. The implications for folding properties and biological significance are discussed.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|