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NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution.
J Am Chem Soc. 2007 May 23; 129(20):6461-9.JA

Abstract

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.

Authors+Show Affiliations

Nikolaev Y
Laboratory of Physical Chemistry, Swiss Federal Institute of Technology (ETH Zurich), CH-8093 Zurich, Switzerland.
Pervushin K
No affiliation info available

MeSH

Amino Acid SequenceBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsHydrogen-Ion ConcentrationLeucine ZippersModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolutionsTranscription Factors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17469817

Citation

Nikolaev, Yaroslav, and Konstantin Pervushin. "NMR Spin State Exchange Spectroscopy Reveals Equilibrium of Two Distinct Conformations of Leucine Zipper GCN4 in Solution." Journal of the American Chemical Society, vol. 129, no. 20, 2007, pp. 6461-9.
Nikolaev Y, Pervushin K. NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution. J Am Chem Soc. 2007;129(20):6461-9.
Nikolaev, Y., & Pervushin, K. (2007). NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution. Journal of the American Chemical Society, 129(20), 6461-9.
Nikolaev Y, Pervushin K. NMR Spin State Exchange Spectroscopy Reveals Equilibrium of Two Distinct Conformations of Leucine Zipper GCN4 in Solution. J Am Chem Soc. 2007 May 23;129(20):6461-9. PubMed PMID: 17469817.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - NMR spin state exchange spectroscopy reveals equilibrium of two distinct conformations of leucine zipper GCN4 in solution. AU - Nikolaev,Yaroslav, AU - Pervushin,Konstantin, Y1 - 2007/05/01/ PY - 2007/5/2/pubmed PY - 2007/9/11/medline PY - 2007/5/2/entrez SP - 6461 EP - 9 JF - Journal of the American Chemical Society JO - J Am Chem Soc VL - 129 IS - 20 N2 - 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. SN - 0002-7863 UR - https://www.unboundmedicine.com/medline/citation/17469817/NMR_spin_state_exchange_spectroscopy_reveals_equilibrium_of_two_distinct_conformations_of_leucine_zipper_GCN4_in_solution_ L2 - https://doi.org/10.1021/ja0685295 DB - PRIME DP - Unbound Medicine ER -