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| | <StructureSection load='5fir' size='340' side='right'caption='[[5fir]], [[Resolution|resolution]] 2.84Å' scene=''> | | <StructureSection load='5fir' size='340' side='right'caption='[[5fir]], [[Resolution|resolution]] 2.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fir]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fir]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIR 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]] 2.836Å</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XRN-2, Y48B6A.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), PAXT-1, CELE_R05D11.6, R05D11.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=5fir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fir OCA], [https://pdbe.org/5fir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fir RCSB], [https://www.ebi.ac.uk/pdbsum/5fir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fir ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fir OCA], [http://pdbe.org/5fir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fir RCSB], [http://www.ebi.ac.uk/pdbsum/5fir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fir ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/XRN2_CAEEL XRN2_CAEEL]] Possesses 5'->3' exoribonuclease activity. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA. Partially redundant to xrn-1 in miRNA guide strand degradation. Implicated in differential regulation of mRNAs such as let-7 by controlling the accumulation of mature miRNA. Positively regulates molting of the pharyngeal cuticle.<ref>PMID:19734881</ref> <ref>PMID:21397849</ref> | + | [https://www.uniprot.org/uniprot/XRN2_CAEEL XRN2_CAEEL] Possesses 5'->3' exoribonuclease activity. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA. Partially redundant to xrn-1 in miRNA guide strand degradation. Implicated in differential regulation of mRNAs such as let-7 by controlling the accumulation of mature miRNA. Positively regulates molting of the pharyngeal cuticle.<ref>PMID:19734881</ref> <ref>PMID:21397849</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: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grosshans, H]] | + | [[Category: Grosshans H]] |
| - | [[Category: Gut, H]] | + | [[Category: Gut H]] |
| - | [[Category: Katic, I]] | + | [[Category: Katic I]] |
| - | [[Category: Richter, H]] | + | [[Category: Richter H]] |
| - | [[Category: 5'-3' exoribonuclease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mirna turnover]]
| + | |
| Structural highlights
Function
XRN2_CAEEL Possesses 5'->3' exoribonuclease activity. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA. Partially redundant to xrn-1 in miRNA guide strand degradation. Implicated in differential regulation of mRNAs such as let-7 by controlling the accumulation of mature miRNA. Positively regulates molting of the pharyngeal cuticle.[1] [2]
Publication Abstract from PubMed
The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate.
Structural basis and function of XRN2 binding by XTB domains.,Richter H, Katic I, Gut H, Grosshans H Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3155. PMID:26779609[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee S, Grosshans H. Active turnover modulates mature microRNA activity in Caenorhabditis elegans. Nature. 2009 Sep 24;461(7263):546-9. doi: 10.1038/nature08349. Epub 2009 Sep 6. PMID:19734881 doi:http://dx.doi.org/10.1038/nature08349
- ↑ Chatterjee S, Fasler M, Bussing I, Grosshans H. Target-mediated protection of endogenous microRNAs in C. elegans. Dev Cell. 2011 Mar 15;20(3):388-96. doi: 10.1016/j.devcel.2011.02.008. PMID:21397849 doi:http://dx.doi.org/10.1016/j.devcel.2011.02.008
- ↑ Richter H, Katic I, Gut H, Grosshans H. Structural basis and function of XRN2 binding by XTB domains. Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3155. PMID:26779609 doi:http://dx.doi.org/10.1038/nsmb.3155
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