1wcl

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{{Seed}}
 
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[[Image:1wcl.png|left|200px]]
 
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==NMR structure of the carboxyterminal domains of Escherichia coli NusA==
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The line below this paragraph, containing "STRUCTURE_1wcl", creates the "Structure Box" on the page.
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<StructureSection load='1wcl' size='340' side='right'caption='[[1wcl]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1wcl]] 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=1WCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCL FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcl OCA], [https://pdbe.org/1wcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcl RCSB], [https://www.ebi.ac.uk/pdbsum/1wcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcl ProSAT]</span></td></tr>
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{{STRUCTURE_1wcl| PDB=1wcl | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wc/1wcl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1wcl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1wcl" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15987884}}, adds the Publication Abstract to the page
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15987884 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15987884}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1WCL is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCL OCA].
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==Reference==
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<ref group="xtra">PMID:15987884</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Eisenmann, A.]]
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[[Category: Large Structures]]
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[[Category: Roesch, P.]]
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[[Category: Eisenmann A]]
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[[Category: Schwarz, S.]]
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[[Category: Roesch P]]
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[[Category: Schweimer, K.]]
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[[Category: Schwarz S]]
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[[Category: C-terminal repeat unit]]
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[[Category: Schweimer K]]
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[[Category: Escherichia coli nusa]]
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[[Category: Nmr]]
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[[Category: Regulation of rna binding]]
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[[Category: Transcription antitermination and termination]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:50:50 2009''
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Current revision

NMR structure of the carboxyterminal domains of Escherichia coli NusA

PDB ID 1wcl

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