4fxe - Revision history

OCA at 11:23, 1 March 2024

OCA — Fri, 01 Mar 2024 11:23:57 GMT

←Older revision		Revision as of 11:23, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXE FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.7503Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [https://pdbe.org/4fxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [https://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [https://pdbe.org/4fxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [https://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The bacterial relBE locus encodes a toxin-antitoxin complex in which the toxin, RelE, is capable of cleaving mRNA in the ribosomal A site cotranslationally. The antitoxin, RelB, both binds and inhibits RelE, and regulates transcription through operator binding and conditional cooperativity controlled by RelE. Here, we present the crystal structure of the intact Escherichia coli RelB2E2 complex at 2.8 A resolution, comprising both the RelB-inhibited RelE and the RelB dimerization domain that binds DNA. RelE and RelB associate into a V-shaped heterotetrameric complex with the ribbon-helix-helix (RHH) dimerization domain at the apex. Our structure supports a model in which relO is optimally bound by two adjacent RelB2E heterotrimeric units, and is not compatible with concomitant binding of two RelB2E2 heterotetramers. The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level.
-
-	The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity.,Boggild A, Sofos N, Andersen KR, Feddersen A, Easter AD, Passmore LA, Brodersen DE Structure. 2012 Oct 10;20(10):1641-8. doi: 10.1016/j.str.2012.08.017. Epub 2012, Sep 13. PMID:22981948<ref>PMID:22981948</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4fxe" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:14, 19 October 2022

OCA — Wed, 19 Oct 2022 20:14:19 GMT

←Older revision		Revision as of 20:14, 19 October 2022
Line 1:		Line 1:

	==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex==		==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex==
-	<StructureSection load='4fxe' size='340' side='right' caption='[[4fxe]], [[Resolution\|resolution]] 2.75Å' scene=''>	+	<StructureSection load='4fxe' size='340' side='right'caption='[[4fxe]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXE FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kha\|3kha]], [[2kc8\|2kc8]], [[2kc9\|2kc9]], [[2k29\|2k29]]</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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [https://pdbe.org/4fxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [https://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1564, JW1556, relB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b1563, JW1555, relE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+
-	<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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [~~http~~://pdbe.org/4fxe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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> [[http://www.uniprot.org/uniprot/RELE_ECOLI RELE_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). Acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl-tRNA in the P site as well as on free 30S subunits. Overexpression of RelE results in the inhibition of bacterial growth and a sharp decrease in colony-forming ability which is inhibited by the labile cognate antitoxin RelB. Overexpression also sharply increases persisters (cells that neither grow or die in presence of bactericidal agent and are largely responsible for high levels of biofilm tolerance to antimicrobials). Acts with RelB as a corepressor of relBE transcription.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:12526800</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:12526800</ref> <ref>PMID:19707553</ref>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Boggild, A~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Brodersen, D E~~]]	+	[[Category: Boggild A]]
-	[[Category: ~~Sofos, N~~]]	+	[[Category: Brodersen DE]]
-	[[Category: ~~Nuclease]]~~	+	[[Category: Sofos N]]
-	~~[[Category: Relb]]~~	+
-	~~[[Category: Rele]]~~	+
-	~~[[Category: Ribosome]]~~	+
-	~~[[Category: Stress response]]~~	+
-	~~[[Category: Toxin]]~~	+
-	~~[[Category: Toxin-toxin inhibitor complex]]~~	+
-	~~[[Category: Toxin/antitoxin system]]~~	+
-	~~[[Category: Translational control~~]]	+

OCA at 19:33, 5 August 2016

OCA — Fri, 05 Aug 2016 19:33:40 GMT

←Older revision		Revision as of 19:33, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex==		==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex==
	<StructureSection load='4fxe' size='340' side='right' caption='[[4fxe]], [[Resolution\|resolution]] 2.75Å' scene=''>		<StructureSection load='4fxe' size='340' side='right' caption='[[4fxe]], [[Resolution\|resolution]] 2.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12 Escherichia coli k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FXE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FXE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kha\|3kha]], [[2kc8\|2kc8]], [[2kc9\|2kc9]], [[2k29\|2k29]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kha\|3kha]], [[2kc8\|2kc8]], [[2kc9\|2kc9]], [[2k29\|2k29]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1564, JW1556, relB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~]), b1563, JW1555, relE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1564, JW1556, relB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b1563, JW1555, relE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-	<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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [http://www.ebi.ac.uk/pdbsum/4fxe PDBsum]</span></td></tr>	+	<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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [http://pdbe.org/4fxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [http://www.ebi.ac.uk/pdbsum/4fxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4fxe" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Boggild, A]]		[[Category: Boggild, A]]
	[[Category: Brodersen, D E]]		[[Category: Brodersen, D E]]

OCA at 05:15, 25 December 2014

OCA — Thu, 25 Dec 2014 05:15:20 GMT

←Older revision		Revision as of 05:15, 25 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4fxe.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of the intact E. coli RelBE toxin-antitoxin complex==
		+	<StructureSection load='4fxe' size='340' side='right' caption='[[4fxe]], [[Resolution\|resolution]] 2.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4fxe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FXE FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3kha\|3kha]], [[2kc8\|2kc8]], [[2kc9\|2kc9]], [[2k29\|2k29]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b1564, JW1556, relB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), b1563, JW1555, relE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
		+	<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=4fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fxe RCSB], [http://www.ebi.ac.uk/pdbsum/4fxe PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://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> [[http://www.uniprot.org/uniprot/RELE_ECOLI RELE_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). Acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl-tRNA in the P site as well as on free 30S subunits. Overexpression of RelE results in the inhibition of bacterial growth and a sharp decrease in colony-forming ability which is inhibited by the labile cognate antitoxin RelB. Overexpression also sharply increases persisters (cells that neither grow or die in presence of bactericidal agent and are largely responsible for high levels of biofilm tolerance to antimicrobials). Acts with RelB as a corepressor of relBE transcription.<ref>PMID:9767574</ref> <ref>PMID:11274135</ref> <ref>PMID:11717402</ref> <ref>PMID:12123459</ref> <ref>PMID:12526800</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:12526800</ref> <ref>PMID:19707553</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The bacterial relBE locus encodes a toxin-antitoxin complex in which the toxin, RelE, is capable of cleaving mRNA in the ribosomal A site cotranslationally. The antitoxin, RelB, both binds and inhibits RelE, and regulates transcription through operator binding and conditional cooperativity controlled by RelE. Here, we present the crystal structure of the intact Escherichia coli RelB2E2 complex at 2.8 A resolution, comprising both the RelB-inhibited RelE and the RelB dimerization domain that binds DNA. RelE and RelB associate into a V-shaped heterotetrameric complex with the ribbon-helix-helix (RHH) dimerization domain at the apex. Our structure supports a model in which relO is optimally bound by two adjacent RelB2E heterotrimeric units, and is not compatible with concomitant binding of two RelB2E2 heterotetramers. The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level.

-	~~{{STRUCTURE_4fxe\| PDB=4fxe \| SCENE= }}~~	+	The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity.,Boggild A, Sofos N, Andersen KR, Feddersen A, Easter AD, Passmore LA, Brodersen DE Structure. 2012 Oct 10;20(10):1641-8. doi: 10.1016/j.str.2012.08.017. Epub 2012, Sep 13. PMID:22981948<ref>PMID:22981948</ref>

-	~~===Crystal structure~~ of the ~~intact E~~. ~~coli RelBE toxin-antitoxin complex===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_22981948}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4fxe]] is a 6 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA].~~	+	</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
-	[[Category: Boggild, A.]]	+	[[Category: Boggild, A]]
-	[[Category: Brodersen, D E.]]	+	[[Category: Brodersen, D E]]
-	[[Category: Sofos, N.]]	+	[[Category: Sofos, N]]
	[[Category: Nuclease]]		[[Category: Nuclease]]
	[[Category: Relb]]		[[Category: Relb]]

OCA at 07:00, 2 January 2013

OCA — Wed, 02 Jan 2013 07:00:33 GMT

←Older revision		Revision as of 07:00, 2 January 2013
Line 1:		Line 1:
-	[[Image:4fxe.~~jpg~~\|left\|200px]]	+	[[Image:4fxe.png\|left\|200px]]

	{{STRUCTURE_4fxe\| PDB=4fxe \| SCENE= }}		{{STRUCTURE_4fxe\| PDB=4fxe \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of the intact E. coli RelBE toxin-antitoxin complex===		===Crystal structure of the intact E. coli RelBE toxin-antitoxin complex===

		+	{{ABSTRACT_PUBMED_22981948}}

	==About this Structure==		==About this Structure==
-	[[4fxe]] is a 6 chain structure with 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=4FXE OCA].	+	[[4fxe]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXE OCA].
-	[[Category: Escherichia coli]]	+	[[Category: Escherichia coli k-12]]
	[[Category: Boggild, A.]]		[[Category: Boggild, A.]]
	[[Category: Brodersen, D E.]]		[[Category: Brodersen, D E.]]

OCA at 05:28, 29 August 2012

OCA — Wed, 29 Aug 2012 05:28:51 GMT

←Older revision		Revision as of 05:28, 29 August 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4fxe.jpg\|left\|200px]]

-	~~The entry~~ 4fxe ~~is ON HOLD~~	+	{{STRUCTURE_4fxe\| PDB=4fxe \| SCENE= }}

-	~~Authors: Brodersen, D.~~E.~~, Boggild, A., Sofos, N.~~	+	===Crystal structure of the intact E. coli RelBE toxin-antitoxin complex===

-	~~Description: Crystal~~ structure ~~of the intact E~~. coli ~~RelBE toxin~~-~~antitoxin~~ complex	+
		+	==About this Structure==
		+	[[4fxe]] is a 6 chain structure with 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=4FXE OCA].
		+	[[Category: Escherichia coli]]
		+	[[Category: Boggild, A.]]
		+	[[Category: Brodersen, D E.]]
		+	[[Category: Sofos, N.]]
		+	[[Category: Nuclease]]
		+	[[Category: Relb]]
		+	[[Category: Rele]]
		+	[[Category: Ribosome]]
		+	[[Category: Stress response]]
		+	[[Category: Toxin]]
		+	[[Category: Toxin-toxin inhibitor complex]]
		+	[[Category: Toxin/antitoxin system]]
		+	[[Category: Translational control]]

OCA: Protected "4fxe" [edit=sysop:move=sysop]

OCA — Wed, 11 Jul 2012 07:52:37 GMT

Protected "4fxe" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:52, 11 July 2012

OCA: New page: '''Unreleased structure''' The entry 4fxe is ON HOLD Authors: Brodersen, D.E., Boggild, A., Sofos, N. Description: Crystal structure of the intact E. coli RelBE toxin-antitoxin complex

OCA — Wed, 11 Jul 2012 07:52:36 GMT

New page: '''Unreleased structure''' The entry 4fxe is ON HOLD Authors: Brodersen, D.E., Boggild, A., Sofos, N. Description: Crystal structure of the intact E. coli RelBE toxin-antitoxin complex

New page

'''Unreleased structure'''

The entry 4fxe is ON HOLD

Authors: Brodersen, D.E., Boggild, A., Sofos, N.

Description: Crystal structure of the intact E. coli RelBE toxin-antitoxin complex