2EVI
Structure of a Ndt80-DNA complex (MSE mutant mA8T)
2EVI の概要
エントリーDOI | 10.2210/pdb2evi/pdb |
関連するPDBエントリー | 1M6U 1M7U 1MN4 1MNN 2EHJ 2ETW 2EUV 2EUW 2EUX 2EUZ 2EVF 2EVG 2EVH |
分子名称 | 5'-D(*TP*GP*CP*GP*AP*CP*AP*CP*AP*AP*TP*AP*AP*C)-3', 5'-D(*AP*GP*TP*TP*AP*TP*TP*GP*TP*GP*TP*CP*GP*C)-3', NDT80 protein, ... (4 entities in total) |
機能のキーワード | beta-barrel, ig-fold transcription factor, cell cycle-dna complex, cell cycle/dna |
由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
細胞内の位置 | Nucleus : P38830 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 48150.13 |
構造登録者 | |
主引用文献 | Lamoureux, J.S.,Glover, J.N. Principles of Protein-DNA Recognition Revealed in the Structural Analysis of Ndt80-MSE DNA Complexes. Structure, 14:555-565, 2006 Cited by PubMed 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. PubMed: 16531239DOI: 10.1016/j.str.2005.11.017 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード