2XCJ
Crystal structure of P2 C, the immunity repressor of temperate E. coli phage P2
2XCJ の概要
| エントリーDOI | 10.2210/pdb2xcj/pdb |
| 分子名称 | C PROTEIN, SODIUM ION, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | direct repeats, repressor, helix-turn-helix, viral protein |
| 由来する生物種 | ENTEROBACTERIA PHAGE P2 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 22328.99 |
| 構造登録者 | |
| 主引用文献 | Massad, T.,Skaar, K.,Nilsson, H.,Damberg, P.,Henriksson-Peltola, P.,Haggard-Ljungquist, E.,Hogbom, M.,Stenmark, P. Crystal Structure of the P2 C-Repressor: A Binder of Non-Palindromic Direct DNA Repeats. Nucleic Acids Res., 38:7778-, 2010 Cited by PubMed Abstract: As opposed to the vast majority of prokaryotic repressors, the immunity repressor of temperate Escherichia coli phage P2 (C) recognizes non-palindromic direct repeats of DNA rather than inverted repeats. We have determined the crystal structure of P2 C at 1.8 Å. This constitutes the first structure solved from the family of C proteins from P2-like bacteriophages. The structure reveals that the P2 C protein forms a symmetric dimer oriented to bind the major groove of two consecutive turns of the DNA. Surprisingly, P2 C has great similarities to binders of palindromic sequences. Nevertheless, the two identical DNA-binding helixes of the symmetric P2 C dimer have to bind different DNA sequences. Helix 3 is identified as the DNA-recognition motif in P2 C by alanine scanning and the importance for the individual residues in DNA recognition is defined. A truncation mutant shows that the disordered C-terminus is dispensable for repressor function. The short distance between the DNA-binding helices together with a possible interaction between two P2 C dimers are proposed to be responsible for extensive bending of the DNA. The structure provides insight into the mechanisms behind the mutants of P2 C causing dimer disruption, temperature sensitivity and insensitivity to the P4 antirepressor. PubMed: 20639540DOI: 10.1093/NAR/GKQ626 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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