Solution structure of a zinc domain conserved in yeast copper-regulated
transcription factors
Ryan B. Turner1, 3, Danielle L. Smith1, 3, Michael E. Zawrotny1, Michael F. Summers1, Matthew C. Posewitz2
& Dennis R. Winge2
1
Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore, Maryland 21250, USA.
2
University of Utah Health Sciences Center, Salt Lake City, Utah 84132, USA.
3
These authors contributed equally to the structure determination.
The three dimensional structure of the N-terminal domain (residues
1−42) of the copper-responsive transcription factor Amt1 from Candida
glabrata has been determined by two-dimensional 1H-correlated
nuclear magnetic resonance (NMR) methods. The domain contains an array of
zinc-binding residues (Cys-X2-Cys-X8-Cys-X-His) that
is conserved among a family of Cu-responsive transcription factors. The structure
is unlike those of previously characterized zinc finger motifs, and consists
of a three-stranded antiparallel -sheet with two short helical segments
that project from one end of the -sheet. Conserved residues at positions
16, 18 and 19 form a basic patch that may be important for DNA binding.
-sheet with two short helical segments
that project from one end of the 
