2k29: Difference between revisions

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==Structure of the DBD domain of E. coli antitoxin RelB==
The line below this paragraph, containing "STRUCTURE_2k29", creates the "Structure Box" on the page.
<StructureSection load='2k29' size='340' side='right'caption='[[2k29]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2k29]] is a 2 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=2K29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K29 FirstGlance]. <br>
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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=2k29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k29 OCA], [https://pdbe.org/2k29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k29 RCSB], [https://www.ebi.ac.uk/pdbsum/2k29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k29 ProSAT]</span></td></tr>
{{STRUCTURE_2k29|  PDB=2k29  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RELB_ECOLI RELB_ECOLI] Antitoxin component of a toxin-antitoxin (TA) module. Counteracts the effect of RelE via direct protein-protein interaction, enabling the reversion of translation inhibition. Also acts as an autorepressor of relBE transcription. DNA-binding and repression is stronger when complexed with corepressor RelE. Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in starved cells due to degradation of RelB by protease Lon.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:19707553</ref>  Seems to be a principal mediator of cell death in liquid media.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:19707553</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/k2/2k29_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=2k29 ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Escherichia coli chromosomal relBE operon encodes a toxin-antitoxin system, which is autoregulated by its protein products, RelB and RelE. RelB acts as a transcriptional repressor and RelE functions as a cofactor to enhance the repressor activity of RelB. Here, we present the NMR-derived structure of a RelB dimer and show that a RelB dimer recognizes a hexad repeat in the palindromic operator region through a ribbon-helix-helix motif. Our biochemical data show that two weakly associated RelB dimers bind to the adjacent repeats in the 3'-site of the operator (O(R)) at a moderate affinity (K(d), approximately 10(-5) M). However, in the presence of RelE, a RelB tetramer binds two distinct binding sites within the operator region, each with an enhanced affinity (K(d), approximately 10(-6) M for the low-affinity site, O(L), and 10(-8) M for the high-affinity site, O(R)). We propose that the enhanced affinity for the operator element is mediated by a cooperative DNA binding by a pair of RelB dimers and that the interaction between RelB dimers is strongly augmented by the presence of the cognate toxin RelE.


'''Structure of the DBD domain of E. coli antitoxin RelB'''
Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module.,Li GY, Zhang Y, Inouye M, Ikura M J Mol Biol. 2008 Jun 27;380(1):107-19. Epub 2008 Apr 22. PMID:18501926<ref>PMID:18501926</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
2K29 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K29 OCA].
<div class="pdbe-citations 2k29" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ikura, M.]]
[[Category: Ikura M]]
[[Category: Inouye, M.]]
[[Category: Inouye M]]
[[Category: Li, G.]]
[[Category: Li G]]
[[Category: Zhang, Y.]]
[[Category: Zhang Y]]
[[Category: Antitoxin]]
[[Category: Relb]]
[[Category: Repressor]]
[[Category: Ribbon-helix-helix]]
[[Category: Stress response]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:38:25 2008''
Retrieved from "https://proteopedia.org/2k29"