2PEX
Structure of reduced C22S OhrR from Xanthamonas Campestris
2PEX の概要
| エントリーDOI | 10.2210/pdb2pex/pdb |
| 関連するPDBエントリー | 1Z91 1Z9C 2PFB |
| 分子名称 | Transcriptional regulator OhrR, FORMIC ACID (3 entities in total) |
| 機能のキーワード | transcription regulator |
| 由来する生物種 | Xanthomonas campestris |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 34199.05 |
| 構造登録者 | |
| 主引用文献 | Newberry, K.J.,Fuangthong, M.,Panmanee, W.,Mongkolsuk, S.,Brennan, R.G. Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR. Mol.Cell, 28:652-664, 2007 Cited by PubMed Abstract: The Xanthomonas campestris transcription regulator OhrR contains a reactive cysteine residue (C22) that upon oxidation by organic hydroperoxides (OHPs) forms an intersubunit disulphide bond with residue C127'. Such modification induces the expression of a peroxidase that reduces OHPs to their less toxic alcohols. Here, we describe the structures of reduced and OHP-oxidized OhrR, visualizing the structural mechanism of OHP induction. Reduced OhrR takes a canonical MarR family fold with C22 and C127' separated by 15.5 A. OHP oxidation results in the disruption of the Y36'-C22-Y47' interaction network and dissection of helix alpha5, which then allows the 135 degrees rotation and 8.2 A translation of C127', formation of the C22-C127' disulphide bond, and alpha6-alpha6' helix-swapped reconfiguration of the dimer interface. These changes result in the 28 degrees rigid body rotations of each winged helix-turn-helix motif and DNA dissociation. Similar effector-induced rigid body rotations are expected for most MarR family members. PubMed: 18042459DOI: 10.1016/j.molcel.2007.09.016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 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






