2evi | pdb_00002evi
From Proteopedia
Structure of a Ndt80-DNA complex (MSE mutant mA8T)
| ||||||||||||
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Principles of protein-DNA recognition revealed in the structural analysis of Ndt80-MSE DNA complexes.,Lamoureux JS, Glover JN Structure. 2006 Mar;14(3):555-65. PMID:16531239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
Contents | ||||||||||||||||||||
This page was last modified 00:13, 30 September 2014.