7o6l
From Proteopedia
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==Crystal structure of C. elegans ERH-2== | ==Crystal structure of C. elegans ERH-2== | ||
| - | <StructureSection load='7o6l' size='340' side='right'caption='[[7o6l]]' scene=''> | + | <StructureSection load='7o6l' size='340' side='right'caption='[[7o6l]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7o6l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O6L FirstGlance]. <br> |
| - | </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=7o6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6l OCA], [https://pdbe.org/7o6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6l RCSB], [https://www.ebi.ac.uk/pdbsum/7o6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6l ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">erh-2, F35G12.11 ([https://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=7o6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o6l OCA], [https://pdbe.org/7o6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o6l RCSB], [https://www.ebi.ac.uk/pdbsum/7o6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o6l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/ERH2_CAEEL ERH2_CAEEL]] Required for chromosome segregation and cell division in early embryos (PubMed:31216475). Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). Promotes the biogenesis of 21U-RNAs (PubMed:31216475).<ref>PMID:31147388</ref> <ref>PMID:31216475</ref> <ref>PMID:31216475</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Piwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. C. elegans piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5' and 3' processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We used biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: PID-1 governs 21U processing, whereas TOST-1 links PETISCO to an unknown process essential for early embryogenesis. Here, we show that PETISCO forms an octameric assembly with each subunit present in two copies. Determination of structures of the TOFU-6/PID-3 and PID-3/ERH-2 subcomplexes, supported by in vivo studies of subunit interaction mutants, allows us to propose a model for the formation of the TOFU-6/PID-3/ERH-2 core complex and its functionality in germ cells and early embryos. Using NMR spectroscopy, we demonstrate that TOST-1 and PID-1 bind to a common surface on ERH-2, located opposite its PID-3 binding site, explaining how PETISCO can mediate different cellular roles. | ||
| + | |||
| + | Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans.,Perez-Borrajero C, Podvalnaya N, Holleis K, Lichtenberger R, Karaulanov E, Simon B, Basquin J, Hennig J, Ketting RF, Falk S Genes Dev. 2021 Sep 1;35(17-18):1304-1323. doi: 10.1101/gad.348648.121. Epub 2021, Aug 19. PMID:34413138<ref>PMID:34413138</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7o6l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Caeel]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Falk S]] | + | [[Category: Falk, S]] |
| - | [[Category: Ketting | + | [[Category: Ketting, R F]] |
| + | [[Category: Enhancer of rudimentary erh homodimer]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 05:56, 6 October 2021
Crystal structure of C. elegans ERH-2
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