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Metal ion co‐ordination in the DNA binding domain of the yeast transcriptional activator GAL4
Author(s) -
Povey Jane F.,
Diakun Gregory P.,
Garner C.David,
Wilson Stephen P.,
Laue Ernest D.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81525-s
Subject(s) - dna binding domain , zinc finger , activator (genetics) , chemistry , yeast , dna , transcription factor , xenopus , transcription (linguistics) , metal , dna binding protein , binding domain , cadmium , biochemistry , microbiology and biotechnology , crystallography , biology , binding site , gene , linguistics , philosophy , organic chemistry
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.