2k29

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[[Image:2k29.png|left|200px]]
 
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{{STRUCTURE_2k29| PDB=2k29 | SCENE= }}
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==Structure of the DBD domain of E. coli antitoxin RelB==
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<StructureSection load='2k29' size='340' side='right'caption='[[2k29]]' scene=''>
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== Structural highlights ==
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<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>
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</table>
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== Function ==
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[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>
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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/k2/2k29_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=2k29 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 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.
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===Structure of the DBD domain of E. coli antitoxin RelB===
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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>
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{{ABSTRACT_PUBMED_18501926}}
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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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==About this Structure==
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<div class="pdbe-citations 2k29" style="background-color:#fffaf0;"></div>
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[[2k29]] is a 2 chain structure with 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=2K29 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:018501926</ref><references group="xtra"/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Ikura, M.]]
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[[Category: Large Structures]]
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[[Category: Inouye, M.]]
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[[Category: Ikura M]]
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[[Category: Li, G.]]
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[[Category: Inouye M]]
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[[Category: Zhang, Y.]]
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[[Category: Li G]]
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[[Category: Antitoxin]]
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[[Category: Zhang Y]]
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[[Category: Relb]]
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[[Category: Repressor]]
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[[Category: Ribbon-helix-helix]]
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[[Category: Stress response]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Structure of the DBD domain of E. coli antitoxin RelB

PDB ID 2k29

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