2ERE
Crystal Structure of a Leu3 DNA-binding domain complexed with a 15mer DNA duplex
Summary for 2ERE
| Entry DOI | 10.2210/pdb2ere/pdb |
| Related | 2ER8 2ERG |
| Descriptor | 5'-D(*TP*TP*GP*CP*CP*GP*GP*TP*AP*CP*CP*GP*GP*CP*A)-3', Regulatory protein LEU3, ZINC ION, ... (4 entities in total) |
| Functional Keywords | zn(2)cys(6)binuclear cluster motif, transcription activator-dna complex, transcription activator/dna |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P08638 |
| Total number of polymer chains | 4 |
| Total formula weight | 26625.68 |
| Authors | Fitzgerald, M.X.,Marmorstein, R. (deposition date: 2005-10-24, release date: 2006-04-04, Last modification date: 2023-08-23) |
| Primary citation | Fitzgerald, M.X.,Rojas, J.R.,Kim, J.M.,Kohlhaw, G.B.,Marmorstein, R. Structure of a Leu3-DNA complex: recognition of everted CGG half-sites by a Zn2Cys6 binuclear cluster protein. Structure, 14:725-735, 2006 Cited by PubMed Abstract: Gal4 is the prototypical Zn2Cys6 binuclear cluster transcriptional regulator that binds as a homodimer to DNA containing inverted CGG half-sites. Leu3, a member of this protein family, binds to everted (opposite polarity to inverted) CGG half-sites, and an H50C mutation within the Leu3 Zn2Cys6 binuclear motif abolishes its transcriptional repression function without impairing DNA binding. We report the X-ray crystal structures of DNA complexes with Leu3 and Leu3(H50C) and solution DNA binding studies of selected Leu3 mutant proteins. These studies reveal the molecular details of everted CGG half-site recognition, and suggest a role for the H50C mutation in transcriptional repression. Comparison with the Gal4-DNA complex shows an unexpected conservation in the DNA recognition mode of inverted and everted CGG half-sites, and points to a critical function of a linker region between the Zn2Cys6 binuclear cluster and dimerization regions in DNA binding specificity. Broader implications of these findings are discussed. PubMed: 16615914DOI: 10.1016/j.str.2005.11.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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