2lq8
From Proteopedia
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| - | [[Image:2lq8.jpg|left|200px]] | ||
| - | + | ==Domain interaction in Thermotoga maritima NusG== | |
| + | <StructureSection load='2lq8' size='340' side='right'caption='[[2lq8]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lq8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq8 OCA], [https://pdbe.org/2lq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq8 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq8 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 2lq8" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Burmann | + | [[Category: Burmann B]] |
| - | [[Category: Droegemueller | + | [[Category: Droegemueller J]] |
| - | [[Category: Roesch | + | [[Category: Roesch P]] |
| - | [[Category: Schweimer | + | [[Category: Schweimer K]] |
| - | [[Category: Stegmann | + | [[Category: Stegmann C]] |
| - | [[Category: Wahl | + | [[Category: Wahl MC]] |
| - | + | ||
Current revision
Domain interaction in Thermotoga maritima NusG
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