1co4
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(New page: 200px<br /><applet load="1co4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1co4" /> '''SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVE...)
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Revision as of 10:29, 20 November 2007
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SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
Overview
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.
About this Structure
1CO4 is a Single protein structure of sequence from [1] with ZN as ligand. Full crystallographic information is available from OCA.
Reference
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
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