2TDX の概要
| エントリーDOI | 10.2210/pdb2tdx/pdb |
| 分子名称 | DIPHTHERIA TOX REPRESSOR, NICKEL (II) ION (3 entities in total) |
| 機能のキーワード | dna-binding regulatory protein, diphtheria tox repressor, transcription regulation, dna-binding protein, iron-regulated repressor, dna binding protein |
| 由来する生物種 | Corynebacterium diphtheriae |
| 細胞内の位置 | Cytoplasm: P33120 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25479.13 |
| 構造登録者 | White, A.,Ding, X.,Zheng, H.,Schiering, N.,Ringe, D.,Murphy, J.R. (登録日: 1998-06-22, 公開日: 1998-10-14, 最終更新日: 2024-05-22) |
| 主引用文献 | White, A.,Ding, X.,vanderSpek, J.C.,Murphy, J.R.,Ringe, D. Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex. Nature, 394:502-506, 1998 Cited by PubMed Abstract: The virulent phenotype of the pathogenic bacterium Corynebacterium diphtheriae is conferred by diphtheria toxin, whose expression is an adaptive response to low concentrations of iron. The expression of the toxin gene (tox) is regulated by the repressor DtxR, which is activated by transition metal ions. X-ray crystal structures of DtxR with and without (apo-form) its coordinated transition metal ion have established the general architecture of the repressor, identified the location of the metal-binding sites, and revealed a metal-ion-triggered subunit-subunit 'caliper-like' conformational change. Here we report the three-dimensional crystal structure of the complex between a biologically active Ni(II)-bound DtxR(C102D) mutant, in which a cysteine is replaced by an aspartate at residue 102, and a 33-base-pair DNA segment containing the toxin operator toxO. This structure shows that DNA interacts with two dimeric repressor proteins bound to opposite sides of the tox operator. We propose that a metal-ion-induced helix-to-coil structural transition in the amino-terminal region of the protein is partly responsible for the unique mode of repressor activation by transition metal ions. PubMed: 9697776DOI: 10.1038/28893 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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