2xhc: Difference between revisions
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< | ==Crystal Structure of Thermotoga maritima N-utilization Substance G (NusG)== | ||
<StructureSection load='2xhc' size='340' side='right'caption='[[2xhc]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xhc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XHC FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | ||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhc OCA], [https://pdbe.org/2xhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xhc RCSB], [https://www.ebi.ac.uk/pdbsum/2xhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xhc ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NUSG_THEMA NUSG_THEMA] Influences transcription termination and antitermination. Acts as a component of the transcription complex, and interacts with the termination factor rho and RNA polymerase (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
An Autoinhibited State in the Structure of Thermotoga maritima NusG.,Drogemuller J, Stegmann CM, Mandal A, Steiner T, Burmann BM, Gottesman ME, Wohrl BM, Rosch P, Wahl MC, Schweimer K Structure. 2013 Feb 12. pii: S0969-2126(13)00008-7. doi:, 10.1016/j.str.2012.12.015. PMID:23415559<ref>PMID:23415559</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
[[ | <div class="pdbe-citations 2xhc" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Stegmann | [[Category: Stegmann CM]] | ||
[[Category: Wahl | [[Category: Wahl MC]] | ||
Latest revision as of 13:31, 20 December 2023
Crystal Structure of Thermotoga maritima N-utilization Substance G (NusG)Crystal Structure of Thermotoga maritima N-utilization Substance G (NusG)
Structural highlights
FunctionNUSG_THEMA Influences transcription termination and antitermination. Acts as a component of the transcription complex, and interacts with the termination factor rho and RNA polymerase (By similarity). Publication Abstract from PubMedNusG 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. An Autoinhibited State in the Structure of Thermotoga maritima NusG.,Drogemuller J, Stegmann CM, Mandal A, Steiner T, Burmann BM, Gottesman ME, Wohrl BM, Rosch P, Wahl MC, Schweimer K Structure. 2013 Feb 12. pii: S0969-2126(13)00008-7. doi:, 10.1016/j.str.2012.12.015. PMID:23415559[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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