2XHA

Crystal Structure of Domain 2 of Thermotoga maritima N-utilization Substance G (NusG)

2XHA の概要

• エントリーDOI: 10.2210/pdb2xha/pdb
• 分子名称: TRANSCRIPTION ANTITERMINATION PROTEIN NUSG, ACETATE ION (3 entities in total)
• 機能のキーワード: transcription
• 由来する生物種: THERMOTOGA MARITIMA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44646.66

構造登録者

Stegmann, C.M.,Mandal, A.,Wahl, M.C. (登録日: 2010-06-11, 公開日: 2011-06-29, 最終更新日: 2024-05-08)

主引用文献

Drogemuller, J.,Stegmann, C.M.,Mandal, A.,Steiner, T.,Burmann, B.M.,Gottesman, M.E.,Wohrl, B.M.,Rosch, P.,Wahl, M.C.,Schweimer, K.
An Autoinhibited State in the Structure of Thermotoga Maritima Nusg.
Structure, 21:365-, 2013

PubMed Abstract: NusG is a conserved regulatory protein interacting with RNA polymerase (RNAP) and other proteins to form multicomponent complexes that modulate transcription. The crystal structure of Thermotoga maritima NusG (TmNusG) shows a three-domain architecture, comprising well-conserved amino-terminal (NTD) and carboxy-terminal (CTD) domains with an additional, species-specific domain inserted into the NTD. NTD and CTD directly contact each other, occluding a surface of the NTD for binding to RNAP and a surface on the CTD interacting either with transcription termination factor Rho or transcription antitermination factor NusE. NMR spectroscopy confirmed the intramolecular NTD-CTD interaction up to the optimal growth temperature of Thermotoga maritima. The domain interaction involves a dynamic equilibrium between open and closed states and contributes significantly to the overall fold stability of the protein. Wild-type TmNusG and deletion variants could not replace endogenous Escherichia coli NusG, suggesting that the NTD-CTD interaction of TmNusG represents an autoinhibited state.

PubMed: 23415559
DOI: 10.1016/J.STR.2012.12.015

実験手法

X-RAY DIFFRACTION (1.906 Å)