1TRR
TANDEM BINDING IN CRYSTALS OF A TRP REPRESSOR/OPERATOR HALF-SITE COMPLEX
1TRR の概要
| エントリーDOI | 10.2210/pdb1trr/pdb |
| 分子名称 | DNA (5'-D(*AP*GP*CP*GP*TP*AP*CP*TP*AP*GP*TP*AP*CP*GP*CP*T)-3'), PROTEIN (TRP REPRESSOR), TRYPTOPHAN, ... (4 entities in total) |
| 機能のキーワード | protein-dna complex, transcription-dna complex, transcription/dna |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cytoplasm: P0A881 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 119145.92 |
| 構造登録者 | |
| 主引用文献 | Lawson, C.L.,Carey, J. Tandem binding in crystals of a trp repressor/operator half-site complex. Nature, 366:178-182, 1993 Cited by PubMed Abstract: The crystal structure of trp repressor tandemly bound in a 2:1 complex to a 16-base-pair palindromic DNA containing a central trp operator half-site has been determined and refined to 2.4 A resolution. Despite dramatically different DNA sequence contexts and crystallization conditions, the protein/DNA interface is essentially identical to that seen in the original trp repressor/operator complex structure. Water-mediated sequence recognition by trp repressor is likely to be related to the unusual end-on approach of the recognition helix (E), which allows sharing of the major groove by tandem dimers. The tandem complex model accounts for the mutational sensitivity of all trp operator base pairs. The structure also provides the first detailed view of the tandem interaction, revealing a key role for the amino-terminal arms. PubMed: 8232559DOI: 10.1038/366178a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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