Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors.
The three dimensional structure of the N-terminal domain (residues 1-42) of the copper-responsive transcription factor Amtl 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 beta-sheet with two short helical segments that project from one end of the beta-sheet. Conserved residues at positions 16, 18 and 19 form a basic patch that may be important for DNA binding.
Howard HUghes Medical Institute, University of Maryland Baltimore County 21250, USA.
R B
RB
Turner
D L
DL
Smith
M E
ME
Zawrotny
M F
MF
Summers
M C
MC
Posewitz
D R
DR
Winge
D000595:Amino Acid Sequence; D002175:Candida / Q000737:chemistry*; D003300:Copper / Q000494:pharmacology; D003545:Cysteine / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry*; D005656:Fungal Proteins; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D014157:Transcription Factors / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D014157:Transcription Factors; C069807:AMT1 protein, Candida glabrate; D003300:Copper; D015032:Zinc; D003545:Cysteine