2lq8
From Proteopedia
(Difference between revisions)
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- | + | ==Domain interaction in Thermotoga maritima NusG== | |
- | === | + | <StructureSection load='2lq8' size='340' side='right' caption='[[2lq8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[2lq8]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LQ8 FirstGlance]. <br> | ||
+ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nusG, TM_0453 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lq8 RCSB], [http://www.ebi.ac.uk/pdbsum/2lq8 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <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> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
- | [[Category: Burmann, B | + | [[Category: Burmann, B]] |
- | [[Category: Droegemueller, J | + | [[Category: Droegemueller, J]] |
- | [[Category: Roesch, P | + | [[Category: Roesch, P]] |
- | [[Category: Schweimer, K | + | [[Category: Schweimer, K]] |
- | [[Category: Stegmann, C | + | [[Category: Stegmann, C]] |
- | [[Category: Wahl, M C | + | [[Category: Wahl, M C]] |
[[Category: Transcription]] | [[Category: Transcription]] |
Revision as of 12:24, 18 December 2014
Domain interaction in Thermotoga maritima NusG
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