8B4E
ToxR bacterial transcriptional regulator bound to 25 bp toxT promoter DNA
8B4E の概要
エントリーDOI | 10.2210/pdb8b4e/pdb |
分子名称 | Cholera toxin transcriptional activator, DNA (25-MER) (3 entities in total) |
機能のキーワード | bacterial transcription, activation complex, dna binding protein |
由来する生物種 | Vibrio cholerae 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 40757.93 |
構造登録者 | Canals, A.,Pieretti, S.,Muriel, M.,El Yaman, N.,Fabrega-Ferrer, M.,Perez-Luque, R.,Krukonis, E.S.,Coll, M. (登録日: 2022-09-20, 公開日: 2023-08-09, 最終更新日: 2024-06-19) |
主引用文献 | Canals, A.,Pieretti, S.,Muriel-Masanes, M.,El Yaman, N.,Plecha, S.C.,Thomson, J.J.,Fabrega-Ferrer, M.,Perez-Luque, R.,Krukonis, E.S.,Coll, M. ToxR activates the Vibrio cholerae virulence genes by tethering DNA to the membrane through versatile binding to multiple sites. Proc.Natl.Acad.Sci.USA, 120:e2304378120-e2304378120, 2023 Cited by PubMed Abstract: ToxR, a transmembrane one-component signal transduction factor, lies within a regulatory cascade that results in the expression of ToxT, toxin coregulated pilus, and cholera toxin. While ToxR has been extensively studied for its ability to activate or repress various genes in , here we present the crystal structures of the ToxR cytoplasmic domain bound to DNA at the and promoters. The structures confirm some predicted interactions, yet reveal other unexpected promoter interactions with implications for other potential regulatory roles for ToxR. We show that ToxR is a versatile virulence regulator that recognizes diverse and extensive, eukaryotic-like regulatory DNA sequences, that relies more on DNA structural elements than specific sequences for binding. Using this topological DNA recognition mechanism, ToxR can bind both in tandem and in a twofold inverted-repeat-driven manner. Its regulatory action is based on coordinated multiple binding to promoter regions near the transcription start site, which can remove the repressing H-NS proteins and prepares the DNA for optimal interaction with the RNA polymerase. PubMed: 37428913DOI: 10.1073/pnas.2304378120 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.25 Å) |
構造検証レポート
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