Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex.
Genesis is an HNF-3/fkh homologous protein. By using multi-dimensional NMR techniques, we have obtained the solution structure and backbone dynamics of Genesis complexed with a 17 base-pair DNA. Our results indicate that both the local folding and dynamic properties of Genesis are perturbed when it binds to the DNA site. Our data show that a conserved flexible amino acid sequence (wing 1) makes dynamic contacts to DNA in the complex and a short helix is induced by Genesis-DNA interactions. Our data indicate that, unlike the HNF-3gamma/DNA complex, a magnesium ion is not required in forming the stable Genesis-DNA complex.
Jin
C
C
Department or Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, Chicago, IL, 60612, USA.
Marsden
I
I
Chen
X
X
Liao
X
X
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D051858:Forkhead Transcription Factors; D019077:Helix-Turn-Helix Motifs; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; D051858:Forkhead Transcription Factors; C101757:Foxd3 protein, mouse; D012097:Repressor Proteins; D004247:DNA