Metal ion co‐ordination in the DNA binding domain of the yeast transcriptional activator GAL4

FEBS Letters

Povey, Jane F.²  Diakun, Gregory P.¹  Laue, Ernest D.²  Garner, C.David³  Wilson, Stephen P.³ 

[1] MRC/SERC Biology Support Laboratory, Daresbury Laboratory, Daresbury, Warrington, WA4 4AD UK;Department of Biochemistry, Tennis Court Road, Cambridge, CB2 1QW, UK;Department of Chemistry, University of Manchester, M13 9PL, UK

关键词: GAL4;    Structure;    DNA binding;    Extended X-ray fine structure;    Zinc finger;    Saccharomyces cerevisiae;   

DOI  :  10.1016/0014-5793(90)81525-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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(Il)-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.

【 授权许可】

Unknown