2XHC

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

Summary for 2XHC

• Entry DOI: 10.2210/pdb2xhc/pdb
• Related: 2XHA
• Descriptor: TRANSCRIPTION ANTITERMINATION PROTEIN NUSG (2 entities in total)
• Functional Keywords: transcription
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 1
• Total formula weight: 40263.93

Authors

Stegmann, C.M.,Wahl, M.C. (deposition date: 2010-06-14, release date: 2011-06-29, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.45 Å)