2MT4

Solution structure of the N-terminal domain of NUSA from B. Subtilis

2MT4 の概要

• エントリーDOI: 10.2210/pdb2mt4/pdb
• NMR情報: BMRB: 25148
• 分子名称: Transcription termination/antitermination protein NusA (1 entity in total)
• 機能のキーワード: transcription factor, nusa, rna polymerase, transcription
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P32727
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14019.86

構造登録者

Mobli, M.,Lewis, P.J. (登録日: 2014-08-12, 公開日: 2015-02-18, 最終更新日: 2024-05-15)

主引用文献

Ma, C.,Mobli, M.,Yang, X.,Keller, A.N.,King, G.F.,Lewis, P.J.
RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.
Nucleic Acids Res., 43:2829-2840, 2015

PubMed Abstract: Pausing during transcription elongation is a fundamental activity in all kingdoms of life. In bacteria, the essential protein NusA modulates transcriptional pausing, but its mechanism of action has remained enigmatic. By combining structural and functional studies we show that a helical rearrangement induced in NusA upon interaction with RNA polymerase is the key to its modulatory function. This conformational change leads to an allosteric re-positioning of conserved basic residues that could enable their interaction with an RNA pause hairpin that forms in the exit channel of the polymerase. This weak interaction would stabilize the paused complex and increases the duration of the transcriptional pause. Allosteric spatial re-positioning of regulatory elements may represent a general approach used across all taxa for modulation of transcription and protein-RNA interactions.

PubMed: 25690895
DOI: 10.1093/nar/gkv108

実験手法

SOLUTION NMR