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| | ==Crystal structure of the toxin RnlA from Escherichia coli== | | ==Crystal structure of the toxin RnlA from Escherichia coli== |
| - | <StructureSection load='4i8o' size='340' side='right' caption='[[4i8o]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4i8o' size='340' side='right'caption='[[4i8o]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4i8o]] is a 2 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=4I8O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I8O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4i8o]] is a 2 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=4I8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I8O FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.104Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yfjN, b2630, JW2611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4i8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i8o OCA], [http://pdbe.org/4i8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i8o RCSB], [http://www.ebi.ac.uk/pdbsum/4i8o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i8o 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=4i8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i8o OCA], [https://pdbe.org/4i8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i8o RCSB], [https://www.ebi.ac.uk/pdbsum/4i8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i8o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RNLA_ECOLI RNLA_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA.<ref>PMID:17895580</ref> <ref>PMID:19019153</ref> <ref>PMID:20980243</ref> <ref>PMID:22403819</ref> | + | [https://www.uniprot.org/uniprot/RNLA_ECOLI RNLA_ECOLI] Toxic component of a toxin-antitoxin (TA) module. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA.<ref>PMID:17895580</ref> <ref>PMID:19019153</ref> <ref>PMID:20980243</ref> <ref>PMID:22403819</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Dong, Y H]] | + | [[Category: Large Structures]] |
| - | [[Category: Gao, Z Q]] | + | [[Category: Dong YH]] |
| - | [[Category: Wei, Y]] | + | [[Category: Gao ZQ]] |
| - | [[Category: Zhang, H]] | + | [[Category: Wei Y]] |
| - | [[Category: Toxin]] | + | [[Category: Zhang H]] |
| - | [[Category: Toxin protein]]
| + | |
| Structural highlights
Function
RNLA_ECOLI Toxic component of a toxin-antitoxin (TA) module. A stable (half-life 27.6 minutes) endoribonuclease that in the absence of cognate antitoxin RnlB causes generalized RNA degradation. Degrades late enterobacteria phage T4 mRNAs, protecting the host against T4 reproduction. Activity is inhibited by cognate antitoxin RnlB and by enterobacteria phage T4 protein Dmd. Targets cyaA mRNA.[1] [2] [3] [4]
Publication Abstract from PubMed
Escherichia coli RnlA-RnlB is a newly identified toxin-antitoxin (TA) system that plays a role in bacteriophage resistance. RnlA functions as a toxin with mRNA endoribonuclease activity and the cognate antitoxin RnlB inhibits RnlA toxicity in E. coli cells. Interestingly, T4 phage encodes the antitoxin Dmd, which acts against RnlA to promote its own propagation, suggesting that RnlA-Dmd represents a novel TA system. Here, we have determined the crystal structure of RnlA refined to 2.10 A. RnlA is composed of three independent domains: NTD (N-terminal domain), NRD (N repeated domain) and DBD (Dmd binding domain), which is an organization not previously observed among known toxin structures. Small-angle X-ray scattering (SAXS) analysis revealed that RnlA forms a dimer in solution via interactions between the DBDs from both monomers. The in vitro and in vivo functional studies showed that among the three domains, only the DBD is responsible for recognition and inhibition by Dmd and subcellular location of RnlA. In particular, the helix located at the C-terminus of DBD plays a vital role in binding Dmd. Our comprehensive studies reveal the key region responsible for RnlA toxicity and provide novel insights into its structure-function relationship.
Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance.,Wei Y, Gao ZQ, Otsuka Y, Naka K, Yonesaki T, Zhang H, Dong YH Mol Microbiol. 2013 Sep 30. doi: 10.1111/mmi.12409. PMID:24112600[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Otsuka Y, Koga M, Iwamoto A, Yonesaki T. A role of RnlA in the RNase LS activity from Escherichia coli. Genes Genet Syst. 2007 Aug;82(4):291-9. PMID:17895580
- ↑ Iwamoto A, Lemire S, Yonesaki T. Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia coli. Mol Microbiol. 2008 Dec;70(6):1570-8. doi: 10.1111/j.1365-2958.2008.06504.x. Epub, 2008 Oct 23. PMID:19019153 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06504.x
- ↑ Koga M, Otsuka Y, Lemire S, Yonesaki T. Escherichia coli rnlA and rnlB compose a novel toxin-antitoxin system. Genetics. 2011 Jan;187(1):123-30. doi: 10.1534/genetics.110.121798. Epub 2010 Oct, 26. PMID:20980243 doi:http://dx.doi.org/10.1534/genetics.110.121798
- ↑ Otsuka Y, Yonesaki T. Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli LsoA and RnlA toxins. Mol Microbiol. 2012 Feb;83(4):669-81. PMID:22403819
- ↑ Wei Y, Gao ZQ, Otsuka Y, Naka K, Yonesaki T, Zhang H, Dong YH. Structure-function studies of Escherichia coli RnlA reveal a novel toxin structure involved in bacteriophage resistance. Mol Microbiol. 2013 Sep 30. doi: 10.1111/mmi.12409. PMID:24112600 doi:http://dx.doi.org/10.1111/mmi.12409
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