1A6I
TET REPRESSOR, CLASS D VARIANT
1A6I の概要
| エントリーDOI | 10.2210/pdb1a6i/pdb |
| 分子名称 | TETRACYCLINE REPRESSOR PROTEIN CLASS D (2 entities in total) |
| 機能のキーワード | transcription regulation, repressor, dna-binding |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 24319.69 |
| 構造登録者 | Orth, P.,Cordes, F.,Schnappinger, D.,Hillen, W.,Saenger, W.,Hinrichs, W. (登録日: 1998-02-25, 公開日: 1999-03-02, 最終更新日: 2024-05-22) |
| 主引用文献 | Orth, P.,Cordes, F.,Schnappinger, D.,Hillen, W.,Saenger, W.,Hinrichs, W. Conformational changes of the Tet repressor induced by tetracycline trapping. J.Mol.Biol., 279:439-447, 1998 Cited by PubMed Abstract: The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations. PubMed: 9642048DOI: 10.1006/jmbi.1998.1775 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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