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| - | {{Seed}} | |
| - | [[Image:2a6q.png|left|200px]] | |
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| - | <!--
| + | ==Crystal structure of YefM-YoeB complex== |
| - | The line below this paragraph, containing "STRUCTURE_2a6q", creates the "Structure Box" on the page.
| + | <StructureSection load='2a6q' size='340' side='right'caption='[[2a6q]], [[Resolution|resolution]] 2.05Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2a6q]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6Q FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</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=2a6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6q OCA], [https://pdbe.org/2a6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6q RCSB], [https://www.ebi.ac.uk/pdbsum/2a6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6q ProSAT]</span></td></tr> |
| - | {{STRUCTURE_2a6q| PDB=2a6q | SCENE= }}
| + | </table> |
| - | | + | == Function == |
| - | ===Crystal structure of YefM-YoeB complex===
| + | [https://www.uniprot.org/uniprot/YOEB_ECOLI YOEB_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> Shown in vitro to be an mRNA interferase that requires translation for substrate cleavage; if the mRNA is mutated so as to not be translatable it is no longer cleaved. Cleavage only occurs within translated regions. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> Also shown in vitro to be a translation initiation blocker. Binds to the 70S ribosome and 50S ribosomal subunit; binding is inhibited by hygromycin A and tetracycline, both of which bind to the 30S subunit in the A site. Thus YoeB is located at the interface between 50S and 30S ribosomes and interacts with the A site where it cleaves mRNA, blocking translation initiation.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> |
| - | | + | == Evolutionary Conservation == |
| - | | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | <!-- | + | Check<jmol> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_16109374}}, adds the Publication Abstract to the page
| + | <jmolCheckbox> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 16109374 is the PubMed ID number.
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6q_consurf.spt"</scriptWhenChecked> |
| - | -->
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | {{ABSTRACT_PUBMED_16109374}}
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ==About this Structure== | + | </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=2a6q ConSurf]. |
| - | 2A6Q is a [[Protein complex]] structure of sequences 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=2A6Q OCA].
| + | <div style="clear:both"></div> |
| - | | + | == References == |
| - | ==Reference== | + | <references/> |
| - | Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin., Kamada K, Hanaoka F, Mol Cell. 2005 Aug 19;19(4):497-509. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16109374 16109374]
| + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Protein complex]] | + | [[Category: Large Structures]] |
| - | [[Category: Hanaoka, F.]] | + | [[Category: Hanaoka F]] |
| - | [[Category: Kamada, K.]] | + | [[Category: Kamada K]] |
| - | [[Category: Addiction module]]
| + | |
| - | [[Category: Antitoxin]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Rnase]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Yefm]]
| + | |
| - | [[Category: Yoeb]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:39:28 2008''
| + | |
| Structural highlights
Function
YOEB_ECOLI Toxic component of a toxin-antitoxin (TA) module. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.[1] [2] [3] [4] [5] [6] [7] [8] Shown in vitro to be an mRNA interferase that requires translation for substrate cleavage; if the mRNA is mutated so as to not be translatable it is no longer cleaved. Cleavage only occurs within translated regions. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides.[9] [10] [11] [12] [13] [14] [15] [16] Also shown in vitro to be a translation initiation blocker. Binds to the 70S ribosome and 50S ribosomal subunit; binding is inhibited by hygromycin A and tetracycline, both of which bind to the 30S subunit in the A site. Thus YoeB is located at the interface between 50S and 30S ribosomes and interacts with the A site where it cleaves mRNA, blocking translation initiation.[17] [18] [19] [20] [21] [22] [23] [24]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Cherny I, Gazit E. The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J Biol Chem. 2004 Feb 27;279(9):8252-61. Epub 2003 Dec 14. PMID:14672926 doi:http://dx.doi.org/10.1074/jbc.M308263200
- ↑ Christensen SK, Maenhaut-Michel G, Mine N, Gottesman S, Gerdes K, Van Melderen L. Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol Microbiol. 2004 Mar;51(6):1705-17. PMID:15009896
- ↑ Kedzierska B, Lian LY, Hayes F. Toxin-antitoxin regulation: bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res. 2007;35(1):325-39. Epub 2006 Dec 14. PMID:17170003 doi:http://dx.doi.org/10.1093/nar/gkl1028
- ↑ Christensen-Dalsgaard M, Gerdes K. Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms. Nucleic Acids Res. 2008 Nov;36(20):6472-81. doi: 10.1093/nar/gkn667. Epub 2008, Oct 14. PMID:18854355 doi:http://dx.doi.org/10.1093/nar/gkn667
- ↑ Bailey SE, Hayes F. Influence of operator site geometry on transcriptional control by the YefM-YoeB toxin-antitoxin complex. J Bacteriol. 2009 Feb;191(3):762-72. doi: 10.1128/JB.01331-08. Epub 2008 Nov 21. PMID:19028895 doi:http://dx.doi.org/10.1128/JB.01331-08
- ↑ Zhang Y, Inouye M. The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin. J Biol Chem. 2009 Mar 13;284(11):6627-38. doi: 10.1074/jbc.M808779200. Epub 2009 , Jan 5. PMID:19124462 doi:http://dx.doi.org/10.1074/jbc.M808779200
- ↑ Winther KS, Gerdes K. Ectopic production of VapCs from Enterobacteria inhibits translation and trans-activates YoeB mRNA interferase. Mol Microbiol. 2009 May;72(4):918-30. doi: 10.1111/j.1365-2958.2009.06694.x. Epub, 2009 Apr 14. PMID:19400780 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06694.x
- ↑ Kamada K, Hanaoka F. Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell. 2005 Aug 19;19(4):497-509. PMID:16109374 doi:10.1016/j.molcel.2005.07.004
- ↑ Cherny I, Gazit E. The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J Biol Chem. 2004 Feb 27;279(9):8252-61. Epub 2003 Dec 14. PMID:14672926 doi:http://dx.doi.org/10.1074/jbc.M308263200
- ↑ Christensen SK, Maenhaut-Michel G, Mine N, Gottesman S, Gerdes K, Van Melderen L. Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol Microbiol. 2004 Mar;51(6):1705-17. PMID:15009896
- ↑ Kedzierska B, Lian LY, Hayes F. Toxin-antitoxin regulation: bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res. 2007;35(1):325-39. Epub 2006 Dec 14. PMID:17170003 doi:http://dx.doi.org/10.1093/nar/gkl1028
- ↑ Christensen-Dalsgaard M, Gerdes K. Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms. Nucleic Acids Res. 2008 Nov;36(20):6472-81. doi: 10.1093/nar/gkn667. Epub 2008, Oct 14. PMID:18854355 doi:http://dx.doi.org/10.1093/nar/gkn667
- ↑ Bailey SE, Hayes F. Influence of operator site geometry on transcriptional control by the YefM-YoeB toxin-antitoxin complex. J Bacteriol. 2009 Feb;191(3):762-72. doi: 10.1128/JB.01331-08. Epub 2008 Nov 21. PMID:19028895 doi:http://dx.doi.org/10.1128/JB.01331-08
- ↑ Zhang Y, Inouye M. The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin. J Biol Chem. 2009 Mar 13;284(11):6627-38. doi: 10.1074/jbc.M808779200. Epub 2009 , Jan 5. PMID:19124462 doi:http://dx.doi.org/10.1074/jbc.M808779200
- ↑ Winther KS, Gerdes K. Ectopic production of VapCs from Enterobacteria inhibits translation and trans-activates YoeB mRNA interferase. Mol Microbiol. 2009 May;72(4):918-30. doi: 10.1111/j.1365-2958.2009.06694.x. Epub, 2009 Apr 14. PMID:19400780 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06694.x
- ↑ Kamada K, Hanaoka F. Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell. 2005 Aug 19;19(4):497-509. PMID:16109374 doi:10.1016/j.molcel.2005.07.004
- ↑ Cherny I, Gazit E. The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J Biol Chem. 2004 Feb 27;279(9):8252-61. Epub 2003 Dec 14. PMID:14672926 doi:http://dx.doi.org/10.1074/jbc.M308263200
- ↑ Christensen SK, Maenhaut-Michel G, Mine N, Gottesman S, Gerdes K, Van Melderen L. Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol Microbiol. 2004 Mar;51(6):1705-17. PMID:15009896
- ↑ Kedzierska B, Lian LY, Hayes F. Toxin-antitoxin regulation: bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res. 2007;35(1):325-39. Epub 2006 Dec 14. PMID:17170003 doi:http://dx.doi.org/10.1093/nar/gkl1028
- ↑ Christensen-Dalsgaard M, Gerdes K. Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms. Nucleic Acids Res. 2008 Nov;36(20):6472-81. doi: 10.1093/nar/gkn667. Epub 2008, Oct 14. PMID:18854355 doi:http://dx.doi.org/10.1093/nar/gkn667
- ↑ Bailey SE, Hayes F. Influence of operator site geometry on transcriptional control by the YefM-YoeB toxin-antitoxin complex. J Bacteriol. 2009 Feb;191(3):762-72. doi: 10.1128/JB.01331-08. Epub 2008 Nov 21. PMID:19028895 doi:http://dx.doi.org/10.1128/JB.01331-08
- ↑ Zhang Y, Inouye M. The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin. J Biol Chem. 2009 Mar 13;284(11):6627-38. doi: 10.1074/jbc.M808779200. Epub 2009 , Jan 5. PMID:19124462 doi:http://dx.doi.org/10.1074/jbc.M808779200
- ↑ Winther KS, Gerdes K. Ectopic production of VapCs from Enterobacteria inhibits translation and trans-activates YoeB mRNA interferase. Mol Microbiol. 2009 May;72(4):918-30. doi: 10.1111/j.1365-2958.2009.06694.x. Epub, 2009 Apr 14. PMID:19400780 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06694.x
- ↑ Kamada K, Hanaoka F. Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell. 2005 Aug 19;19(4):497-509. PMID:16109374 doi:10.1016/j.molcel.2005.07.004
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