Structural highlights
Function
AMT1_CANGA Trans-acting regulatory protein that activates transcription of the MT genes (metallothionein) in response to copper or silver ions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors.,Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR. Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors. Nat Struct Biol. 1998 Jul;5(7):551-5. PMID:9665167 doi:10.1038/805
