View source for 1wcn


==NMR structure of the carboxyterminal domains of Escherichia coli NusA==
<StructureSection load='1wcn' size='340' side='right'caption='[[1wcn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCN 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=1wcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcn OCA], [https://pdbe.org/1wcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcn RCSB], [https://www.ebi.ac.uk/pdbsum/1wcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NUSA_ECOLI NUSA_ECOLI] Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.<ref>PMID:6263495</ref> <ref>PMID:6265785</ref> <ref>PMID:6199039</ref> <ref>PMID:2821282</ref> <ref>PMID:7536848</ref> <ref>PMID:9139668</ref> <ref>PMID:11719185</ref> <ref>PMID:20696893</ref> <ref>PMID:21922055</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wc/1wcn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wcn ConSurf].
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== Publication Abstract from PubMed ==
The carboxy-terminal domain of the transcription factor Escherichia coli NusA, NusACTD, interacts with the protein N of bacteriophage lambda, lambdaN, and the carboxyl terminus of the E. coli RNA polymerase alpha subunit, alphaCTD. We solved the solution structure of the unbound NusACTD with high-resolution nuclear magnetic resonance (NMR). Additionally, we investigated the binding sites of lambdaN and alphaCTD on NusACTD using NMR titrations. The solution structure of NusACTD shows two structurally similar subdomains, NusA(353-416) and NusA(431-490), matching approximately two homologous acidic sequence repeats. Further characterization of NusACTD with 15N NMR relaxation data suggests that the interdomain region is only weakly structured and that the subdomains are not interacting. Both subdomains adopt an (HhH)2 fold. These folds are normally involved in DNA-protein and protein-protein interactions. NMR titration experiments show clear differences of the interactions of these two domains with alphaCTD and lambdaN, in spite of their structural similarity.

The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction.,Eisenmann A, Schwarz S, Prasch S, Schweimer K, Rosch P Protein Sci. 2005 Aug;14(8):2018-29. Epub 2005 Jun 29. PMID:15987884<ref>PMID:15987884</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1wcn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Eisenmann A]]
[[Category: Roesch P]]
[[Category: Schwarz S]]
[[Category: Schweimer K]]