2xhc

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{{STRUCTURE_2xhc| PDB=2xhc | SCENE= }}
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==Crystal Structure of Thermotoga maritima N-utilization Substance G (NusG)==
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===Crystal Structure of Thermotoga maritima N-utilization Substance G (NusG)===
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<StructureSection load='2xhc' size='340' side='right' caption='[[2xhc]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23415559}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xhc]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XHC FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xha|2xha]]</td></tr>
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<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=2xhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xhc RCSB], [http://www.ebi.ac.uk/pdbsum/2xhc PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Function==
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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>
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[[http://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).
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2xhc]] is a 1 chain structure with sequence from [http://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].
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Stegmann, C M.]]
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[[Category: Stegmann, C M]]
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[[Category: Wahl, M C.]]
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[[Category: Wahl, M C]]
[[Category: Transcription]]
[[Category: Transcription]]

Revision as of 12:21, 18 December 2014

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

2xhc, resolution 2.45Å

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