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5fir

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==Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1==
==Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1==
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<StructureSection load='5fir' size='340' side='right' caption='[[5fir]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
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<StructureSection load='5fir' size='340' side='right'caption='[[5fir]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5fir]] is a 12 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIR FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.836&#8491;</td></tr>
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<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>
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<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>
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<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=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]</span></td></tr>
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<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>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:26779609</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5fir" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Grosshans, H]]
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[[Category: Caenorhabditis elegans]]
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[[Category: Gut, H]]
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[[Category: Large Structures]]
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[[Category: Katic, I]]
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[[Category: Grosshans H]]
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[[Category: Richter, H]]
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[[Category: Gut H]]
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[[Category: 5'-3' exoribonuclease]]
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[[Category: Katic I]]
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[[Category: Hydrolase]]
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[[Category: Richter H]]
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[[Category: Mirna turnover]]
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Current revision

Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1

PDB ID 5fir

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