1CO4
SOLUTION STRUCTURE OF A ZINC DOMAIN CONSERVED IN YEAST COPPER-REGULATED TRANSCRIPTION FACTORS
Summary for 1CO4
| Entry DOI | 10.2210/pdb1co4/pdb |
| Descriptor | PROTEIN (ACTIVATOR OF METALLOTHIONEIN 1), ZINC ION (2 entities in total) |
| Functional Keywords | metallothionein, amt, metal regulation, translation-regulation protein complex, translation/regulation protein |
| Cellular location | Nucleus: P41772 |
| Total number of polymer chains | 1 |
| Total formula weight | 4751.96 |
| Authors | Turner, R.B.,Smith, D.L.,Zawrotny, M.E.,Summers, M.F.,Posewitz, M.C.,Winge, D.R. (deposition date: 1999-06-04, release date: 1999-06-10, Last modification date: 2023-12-27) |
| Primary citation | Turner, R.B.,Smith, D.L.,Zawrotny, M.E.,Summers, M.F.,Posewitz, M.C.,Winge, D.R. Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors. Nat.Struct.Biol., 5:551-555, 1998 Cited by PubMed Abstract: 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. PubMed: 9665167DOI: 10.1038/805 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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