An autoinhibited state in the structure of Thermotoga maritima NusG.
An autoinhibited state in the structure of Thermotoga maritima NusG.
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DOI:
10.1016/j.str.2012.12.015
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发表时间:
2013-03-05
期刊:
影响因子:
5.7
通讯作者:
Schweimer, Kristian
中科院分区:
文献类型:
--
作者:
Droegemueller, Johanna;Stegmann, Christian M.;Mandal, Angshuman;Steiner, Thomas;Burmann, Bjoern M.;Gottesman, Max E.;Woehrl, Birgitta M.;Roesch, Paul;Wahl, Markus C.;Schweimer, Kristian
NusG is a conserved regulatory protein interacting with RNA polymerase (RNAP) and other proteins to form multi-component 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 anti-termination factor NusE. NMR spectroscopy confirmed the intra-molecular 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 for endogenous Escherichia coli NusG, suggesting that the NTD-CTD interaction of TmNusG represents an auto-inhibited state.
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影响因子:
3.2
作者:
Liao, DQ;Lurz, R;Dennis, PP
通讯作者:
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DOI:
10.1073/pnas.0405883101
发表时间:
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影响因子:
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期刊:
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通讯作者:
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DOI:
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发表时间:
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影响因子:
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通讯作者:
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