Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to resonance overlap and broadened crosspeaks. This approach involved the use of selectively deuteriated, 13C- and 15N-labeled samples and 'isotopic heterodimers' to distinguish between intra- and intermonomeric NOEs. A comparison with the crystal structure and NMR analysis of the E. coli HU protein suggests that other homologous proteins in this family will possess similar tertiary structures. This NMR strategy is applicable to the study of other proteins and their biomolecular complexes.
Hsu
V L
VL
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331-7305, USA.
Jia
X
X
Kearns
D R
DR
D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D014157:Transcription Factors / Q000737:chemistry* / Q000502:physiology
D004268:DNA-Binding Proteins; D014157:Transcription Factors