7qy5

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'''Unreleased structure'''
 
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The entry 7qy5 is ON HOLD until Paper Publication
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==Crystal structure of the S.pombe Ars2-Red1 complex.==
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<StructureSection load='7qy5' size='340' side='right'caption='[[7qy5]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7qy5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QY5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7qy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qy5 OCA], [https://pdbe.org/7qy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qy5 RCSB], [https://www.ebi.ac.uk/pdbsum/7qy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qy5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIR2_SCHPO PIR2_SCHPO]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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To eliminate specific or aberrant transcripts, eukaryotes use nuclear RNA-targeting complexes that deliver them to the exosome for degradation. S. pombe MTREC, and its human counterpart PAXT, are key players in this mechanism but inner workings of these complexes are not understood in sufficient detail. Here, we present an NMR structure of an MTREC scaffold protein Red1 helix-turn-helix domain bound to the Iss10 N-terminus and show this interaction is required for proper cellular growth and meiotic mRNA degradation. We also report a crystal structure of a Red1-Ars2 complex explaining mutually exclusive interactions of hARS2 with various ED/EGEI/L motif-possessing RNA regulators, including hZFC3H1 of PAXT, hFLASH or hNCBP3. Finally, we show that both Red1 and hZFC3H1 homo-dimerize via their coiled-coil regions indicating that MTREC and PAXT likely function as dimers. Our results, combining structures of three Red1 interfaces with in vivo studies, provide mechanistic insights into conserved features of MTREC/PAXT architecture.
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Authors: Foucher, A.E., Kadlec, J.
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Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.,Foucher AE, Touat-Todeschini L, Juarez-Martinez AB, Rakitch A, Laroussi H, Karczewski C, Acajjaoui S, Soler-Lopez M, Cusack S, Mackereth CD, Verdel A, Kadlec J Nat Commun. 2022 Aug 24;13(1):4969. doi: 10.1038/s41467-022-32542-3. PMID:36002457<ref>PMID:36002457</ref>
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Description: Crystal structure of the S.pombe Ars2-Red1 complex.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kadlec, J]]
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<div class="pdbe-citations 7qy5" style="background-color:#fffaf0;"></div>
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[[Category: Foucher, A.E]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Schizosaccharomyces pombe]]
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[[Category: Foucher AE]]
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[[Category: Kadlec J]]

Revision as of 20:04, 16 November 2022

Crystal structure of the S.pombe Ars2-Red1 complex.

PDB ID 7qy5

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