The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator protein.

Liang H, Olejniczak ET, Mao X, Nettesheim DG, Yu L, Thompson CB, Fesik SW
Proc Natl Acad Sci U S A. 1994 91 (24): 11655-9

PMID: 7972119 · PMCID: PMC45290 · DOI:10.1073/pnas.91.24.11655

The ets family of eukaryotic transcription factors is characterized by a conserved DNA-binding domain of approximately 85 amino acids for which the three-dimensional structure is not known. By using multidimensional NMR spectroscopy, we have determined the secondary structure of the ets domain of one member of this gene family, human Fli-1, both in the free form and in a complex with a 16-bp cognate DNA site. The secondary structure of the Fli-1 ets domain consists of three alpha-helices and a short four-stranded antiparallel beta-sheet. This secondary structure arrangement resembles that of the DNA-binding domain of the catabolite gene activator protein of Escherichia coli, as well as those of several eukaryotic DNA-binding proteins including histone H5, HNF-3/fork head, and the heat shock transcription factor. Differences in chemical shifts of backbone resonances and amide exchange rates between the DNA-bound and free forms of the Fli-1 ets domain suggest that the third helix is the DNA recognition helix, as in the catabolite gene activator protein and other structurally related proteins. These results suggest that the ets domain is structurally similar to the catabolite gene activator protein family of helix-turn-helix DNA-binding proteins.

MeSH Terms (17)

Amino Acid Sequence Base Sequence Cyclic AMP Receptor Protein DNA-Binding Proteins Escherichia coli Helix-Loop-Helix Motifs Humans Hydrogen Bonding Magnetic Resonance Spectroscopy Molecular Sequence Data Oligodeoxyribonucleotides Protein Conformation Protein Structure, Secondary Proto-Oncogene Protein c-fli-1 Proto-Oncogene Proteins Recombinant Proteins Trans-Activators

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