5N7Y
Solution structure of B. subtilis Sigma G inhibitor CsfB
5N7Y の概要
エントリーDOI | 10.2210/pdb5n7y/pdb |
NMR情報 | BMRB: 34102 |
分子名称 | Anti-sigma-G factor Gin, ZINC ION (2 entities in total) |
機能のキーワード | zinc-finger, dimer, csfb, sigma g inhibitor, transcription |
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 | 11391.60 |
構造登録者 | Martinez-Lumbreras, S.,Alfano, C.,Atkinson, A.,Isaacson, R.L. (登録日: 2017-02-21, 公開日: 2018-02-28, 最終更新日: 2024-06-19) |
主引用文献 | Martinez-Lumbreras, S.,Alfano, C.,Evans, N.J.,Collins, K.M.,Flanagan, K.A.,Atkinson, R.A.,Krysztofinska, E.M.,Vydyanath, A.,Jackter, J.,Fixon-Owoo, S.,Camp, A.H.,Isaacson, R.L. Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB. Structure, 26:640-648.e5, 2018 Cited by PubMed Abstract: Global changes in bacterial gene expression can be orchestrated by the coordinated activation/deactivation of alternative sigma (σ) factor subunits of RNA polymerase. Sigma factors themselves are regulated in myriad ways, including via anti-sigma factors. Here, we have determined the solution structure of anti-sigma factor CsfB, responsible for inhibition of two alternative sigma factors, σ and σ, during spore formation by Bacillus subtilis. CsfB assembles into a symmetrical homodimer, with each monomer bound to a single Zn ion via a treble-clef zinc finger fold. Directed mutagenesis indicates that dimer formation is critical for CsfB-mediated inhibition of both σ and σ, and we have characterized these interactions in vitro. This work represents an advance in our understanding of how CsfB mediates inhibition of two alternative sigma factors to drive developmental gene expression in a bacterium. PubMed: 29526435DOI: 10.1016/j.str.2018.02.007 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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