7tqv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SARS-CoV-2 endoribonuclease Nsp15 bound to dsRNA== | |
| + | <StructureSection load='7tqv' size='340' side='right'caption='[[7tqv]], [[Resolution|resolution]] 3.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7tqv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TQV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.43Å</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=7tqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tqv OCA], [https://pdbe.org/7tqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tqv RCSB], [https://www.ebi.ac.uk/pdbsum/7tqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tqv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coronaviruses generate double-stranded (ds) RNA intermediates during viral replication that can activate host immune sensors. To evade activation of the host pattern recognition receptor MDA5, coronaviruses employ Nsp15, which is a uridine-specific endoribonuclease. Nsp15 is proposed to associate with the coronavirus replication-transcription complex within double-membrane vesicles to cleave these dsRNA intermediates. How Nsp15 recognizes and processes dsRNA is poorly understood because previous structural studies of Nsp15 have been limited to small single-stranded (ss) RNA substrates. Here we present cryo-EM structures of SARS-CoV-2 Nsp15 bound to a 52nt dsRNA. We observed that the Nsp15 hexamer forms a platform for engaging dsRNA across multiple protomers. The structures, along with site-directed mutagenesis and RNA cleavage assays revealed critical insight into dsRNA recognition and processing. To process dsRNA Nsp15 utilizes a base-flipping mechanism to properly orient the uridine within the active site for cleavage. Our findings show that Nsp15 is a distinctive endoribonuclease that can cleave both ss- and dsRNA effectively. | ||
| - | + | Flipped over U: structural basis for dsRNA cleavage by the SARS-CoV-2 endoribonuclease.,Frazier MN, Wilson IM, Krahn JM, Butay KJ, Dillard LB, Borgnia MJ, Stanley RE Nucleic Acids Res. 2022 Aug 12;50(14):8290-8301. doi: 10.1093/nar/gkac589. PMID:35801916<ref>PMID:35801916</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7tqv" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Uridylate-specific endoribonuclease|Uridylate-specific endoribonuclease]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Severe acute respiratory syndrome coronavirus 2]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Borgnia MJ]] | ||
| + | [[Category: Butay KJ]] | ||
| + | [[Category: Dillard LB]] | ||
| + | [[Category: Frazier MN]] | ||
| + | [[Category: Krahn JM]] | ||
| + | [[Category: Stanley RE]] | ||
Current revision
SARS-CoV-2 endoribonuclease Nsp15 bound to dsRNA
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