2RO5
RDC-refined solution structure of the N-terminal DNA recognition domain of the Bacillus subtilis transition-state regulator SpoVT
2RO5 の概要
エントリーDOI | 10.2210/pdb2ro5/pdb |
関連するPDBエントリー | 1Z0R 2FY9 2RO3 2RO4 |
NMR情報 | BMRB: 11034 |
分子名称 | Stage V sporulation protein T (1 entity in total) |
機能のキーワード | transcription, activator, dna-binding, repressor, sporulation, transcription regulation |
由来する生物種 | Bacillus subtilis |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 12777.06 |
構造登録者 | Sullivan, D.M.,Bobay, B.G.,Kojetin, D.J.,Thompson, R.J.,Rance, M.,Strauch, M.A.,Cavanagh, J. (登録日: 2008-03-08, 公開日: 2008-11-11, 最終更新日: 2024-05-01) |
主引用文献 | Sullivan, D.M.,Bobay, B.G.,Kojetin, D.J.,Thompson, R.J.,Rance, M.,Strauch, M.A.,Cavanagh, J. Insights into the nature of DNA binding of AbrB-like transcription factors Structure, 16:1702-1713, 2008 Cited by PubMed Abstract: Understanding the DNA recognition and binding by the AbrB-like family of transcriptional regulators is of significant interest since these proteins enable bacteria to elicit the appropriate response to diverse environmental stimuli. Although these "transition-state regulator" proteins have been well characterized at the genetic level, the general and specific mechanisms of DNA binding remain elusive. We present RDC-refined NMR solution structures and dynamic properties of the DNA-binding domains of three Bacillus subtilis transition-state regulators: AbrB, Abh, and SpoVT. We combined previously investigated DNase I footprinting, DNA methylation, gel-shift assays, and mutagenic and NMR studies to generate a structural model of the complex between AbrBN(55) and its cognate promoter, abrB8. These investigations have enabled us to generate a model for the specific nature of the transition-state regulator-DNA interaction, a structure that has remained elusive thus far. PubMed: 19000822DOI: 10.1016/j.str.2008.08.014 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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