Summary information and primary citation
- PDB-id
- 2eux; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- cell cycle-DNA
- Method
- X-ray (1.57 Å)
- Summary
- Structure of a ndt80-DNA complex (mse variant va4g)
- Reference
- Lamoureux JS, Glover JN (2006): "Principles of Protein-DNA Recognition Revealed in the Structural Analysis of Ndt80-MSE DNA Complexes." Structure, 14, 555-565. doi: 10.1016/j.str.2005.11.017.
- Abstract
- The Saccharomyces cerevisiae transcription factor Ndt80 selectively binds a DNA consensus sequence (the middle sporulation element [MSE]) to activate gene expression after the successful completion of meiotic recombination. Here we report the X-ray crystal structures of Ndt80 bound to ten distinct MSE variants. Comparison of these structures with the structure of Ndt80 bound to a consensus MSE reveals structural principles that determine the DNA binding specificity of this transcription factor. The 5' GC-rich end of the MSE contains distinct 5'-YpG-3' steps that are recognized by arginine side chains through a combination of hydrogen bonding and cation-pi interactions. The 3' AT-rich region is recognized via minor groove contacts that sterically exclude the N2 atom of GC base pairs. The conformation of the AT-rich region is fixed by interactions with the protein that favor recognition of poly(A)-poly(T) versus mixed AT sequences through an avoidance of major groove steric clashes at 5'-ApT-3' steps.
