2ERG

Crystal Structure of Leu3 DNA-binding domain with a single H50C mutation complexed with a 15mer DNA duplex

Summary for 2ERG

• Entry DOI: 10.2210/pdb2erg/pdb
• Related: 2ER8 2ERE
• 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: 26555.68

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

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: 16615914
DOI: 10.1016/j.str.2005.11.025

Experimental method

X-RAY DIFFRACTION (3.15 Å)