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2ere
From Proteopedia
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Crystal Structure of a Leu3 DNA-binding domain complexed with a 15mer DNA duplex
Overview
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.
About this Structure
2ERE is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of a Leu3-DNA complex: recognition of everted CGG half-sites by a Zn2Cys6 binuclear cluster protein., Fitzgerald MX, Rojas JR, Kim JM, Kohlhaw GB, Marmorstein R, Structure. 2006 Apr;14(4):725-35. PMID:16615914
Page seeded by OCA on Wed Nov 21 10:06:12 2007
