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2kc9

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Revision as of 09:15, 10 September 2015

Structure of E. coli toxin RelE (R81A/R83A) mutant in the free state

Structural highlights

2kc9 is a 1 chain structure with sequence from Ecoli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2kc8
Gene:	relE, b1563, JW1555 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] Seems to be a principal mediator of cell death in liquid media.^[7] ^[8] ^[9] ^[10] ^[11] ^[12]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In Escherichia coli, RelE toxin participates in growth arrest and cell death by inducing mRNA degradation at the ribosomal A-site under stress conditions. The NMR structures of a mutant of E. coli RelE toxin, RelE(R81A/R83A), with reduced toxicity and its complex with an inhibitory peptide from RelB antitoxin, RelB(C) (Lys(47)-Leu(79)), have been determined. In the free RelE(R81A/R83A) structure, helix alpha4 at the C terminus adopts a closed conformation contacting with the beta-sheet core and adjacent loops. In the RelE(R81A/R83A)-RelB(C) complex, helix alpha3(*) of RelB(C) displaces alpha4 of RelE(R81A/R83A) from the binding site on the beta-sheet core. This helix replacement results in neutralization of a conserved positively charged cluster of RelE by acidic residues from alpha3(*) of RelB. The released helix alpha4 becomes unfolded, adopting an open conformation with increased mobility. The displacement of alpha4 disrupts the geometry of critical residues, including Arg(81) and Tyr(87), in a putative active site of RelE toxin. Our structures indicate that RelB counteracts the toxic activity of RelE by displacing alpha4 helix from the catalytically competent position found in the free RelE structure.

Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site.,Li GY, Zhang Y, Inouye M, Ikura M J Biol Chem. 2009 May 22;284(21):14628-36. Epub 2009 Mar 18. PMID:19297318^[13]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gotfredsen M, Gerdes K. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol. 1998 Aug;29(4):1065-76. PMID:9767574
↑ Galvani C, Terry J, Ishiguro EE. Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes. J Bacteriol. 2001 Apr;183(8):2700-3. PMID:11274135 doi:http://dx.doi.org/10.1128/JB.183.8.2700-2703.2001
↑ Christensen SK, Mikkelsen M, Pedersen K, Gerdes K. RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14328-33. Epub 2001 Nov 20. PMID:11717402 doi:http://dx.doi.org/10.1073/pnas.251327898
↑ Pedersen K, Christensen SK, Gerdes K. Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol Microbiol. 2002 Jul;45(2):501-10. PMID:12123459
↑ Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K, Ehrenberg M. The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell. 2003 Jan 10;112(1):131-40. PMID:12526800
↑ Kolodkin-Gal I, Verdiger R, Shlosberg-Fedida A, Engelberg-Kulka H. A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation. PLoS One. 2009 Aug 26;4(8):e6785. doi: 10.1371/journal.pone.0006785. PMID:19707553 doi:10.1371/journal.pone.0006785
↑ Gotfredsen M, Gerdes K. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol. 1998 Aug;29(4):1065-76. PMID:9767574
↑ Galvani C, Terry J, Ishiguro EE. Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes. J Bacteriol. 2001 Apr;183(8):2700-3. PMID:11274135 doi:http://dx.doi.org/10.1128/JB.183.8.2700-2703.2001
↑ Christensen SK, Mikkelsen M, Pedersen K, Gerdes K. RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14328-33. Epub 2001 Nov 20. PMID:11717402 doi:http://dx.doi.org/10.1073/pnas.251327898
↑ Pedersen K, Christensen SK, Gerdes K. Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol Microbiol. 2002 Jul;45(2):501-10. PMID:12123459
↑ Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K, Ehrenberg M. The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell. 2003 Jan 10;112(1):131-40. PMID:12526800
↑ Kolodkin-Gal I, Verdiger R, Shlosberg-Fedida A, Engelberg-Kulka H. A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation. PLoS One. 2009 Aug 26;4(8):e6785. doi: 10.1371/journal.pone.0006785. PMID:19707553 doi:10.1371/journal.pone.0006785
↑ Li GY, Zhang Y, Inouye M, Ikura M. Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. J Biol Chem. 2009 May 22;284(21):14628-36. Epub 2009 Mar 18. PMID:19297318 doi:10.1074/jbc.M809656200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kc9"

@@ Line 2: / Line 2: @@
 <StructureSection load='2kc9' size='340' side='right' caption='[[2kc9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kc9]] is a 1 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=2KC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KC9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kc9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KC9 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kc8|2kc8]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">relE, b1563, JW1555 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">relE, b1563, JW1555 ([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=2kc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kc9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kc9 RCSB], [http://www.ebi.ac.uk/pdbsum/2kc9 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=2kc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kc9 OCA], [http://pdbe.org/2kc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kc9 RCSB], [http://www.ebi.ac.uk/pdbsum/2kc9 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2kc9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Ecoli]]
 [[Category: Ikura, M]]
 [[Category: Inouye, M]]

2kc9

From Proteopedia

Revision as of 09:15, 10 September 2015

Structure of E. coli toxin RelE (R81A/R83A) mutant in the free state

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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