Metal ion co-ordination in the DNA binding domain of the yeast transcriptional activator GAL4.
The structure of the DNA binding domain of the yeast transcriptional activator GAL4 was investigated by extended X-ray fine structure (e.x.a.f.s.). Two samples of GAL4 were studied, one containing cadmium as a structural probe (Cd(II)GAL4) and the other containing the 'native' zinc (Zn(II)-GAL4). The results suggest that the structure of the DNA binding domain of GAL4 contains a two metal ion cluster distinguishing it from the 'zinc finger' proteins typified by the Xenopus laevis transcription factor TFIIIA.
Department of Biochemistry, Cambridge, UK.
J F
JF
Povey
G P
GP
Diakun
C D
CD
Garner
S P
SP
Wilson
E D
ED
Laue
D002104:Cadmium; D002413:Cations, Divalent; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000648:ultrastructure*; D005583:Fourier Analysis; D005656:Fungal Proteins / Q000378:metabolism / Q000648:ultrastructure*; D066298:In Vitro Techniques; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013057:Spectrum Analysis; D013455:Sulfur; D014157:Transcription Factors / Q000378:metabolism / Q000648:ultrastructure*; D014965:X-Rays; D015032:Zinc
D002413:Cations, Divalent; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C052130:GAL4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D002104:Cadmium; D013455:Sulfur; D015032:Zinc