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7yev
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7yev is ON HOLD Authors: Bao, K.Y., Zhang, X.L., Li, D.Y., Zhu, P. Description: In situ structure of polymerase complex of mammalian reovirus in th...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==In situ structure of polymerase complex of mammalian reovirus in the pre-elongation state== | |
| + | <StructureSection load='7yev' size='340' side='right'caption='[[7yev]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7yev]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3 Mammalian orthoreovirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YEV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7yev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yev OCA], [https://pdbe.org/7yev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yev RCSB], [https://www.ebi.ac.uk/pdbsum/7yev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yev ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mammalian reovirus (reovirus) is a multilayered, turreted member of Reoviridae characterized by transcription of dsRNA genome within the innermost capsid shell. Here, we present high-resolution in situ structures of reovirus transcriptase complex in an intact double-layered virion, and in the uncoated single-layered core particles in the unloaded, reloaded, pre-elongation, and elongation states, respectively, obtained by cryo-electron microscopy and sub-particle reconstructions. At the template entry of RNA-dependent RNA polymerase (RdRp), the RNA-loading region gets flexible after uncoating resulting in the unloading of terminal genomic RNA and inactivity of transcription. However, upon adding transcriptional substrates, the RNA-loading region is recovered leading the RNAs loaded again. The priming loop in RdRp was found to play a critical role in regulating transcription, which hinders the elongation of transcript in virion and triggers the rearrangement of RdRp C-terminal domain (CTD) during elongation, resulting in splitting of template-transcript hybrid and opening of transcript exit. With the integration of these structures, a transcriptional model of reovirus with five states is proposed. Our structures illuminate the RdRp activation and regulation of the multilayered turreted reovirus. | ||
| - | + | In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.,Bao K, Zhang X, Li D, Sun W, Sun Z, Wang J, Zhu P Proc Natl Acad Sci U S A. 2022 Dec 13;119(50):e2203054119. doi: , 10.1073/pnas.2203054119. Epub 2022 Dec 5. PMID:36469786<ref>PMID:36469786</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bao | + | <div class="pdbe-citations 7yev" style="background-color:#fffaf0;"></div> |
| - | [[Category: Li | + | == References == |
| - | [[Category: Zhang | + | <references/> |
| - | [[Category: Zhu | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mammalian orthoreovirus 3]] | ||
| + | [[Category: Bao KY]] | ||
| + | [[Category: Li DY]] | ||
| + | [[Category: Zhang XL]] | ||
| + | [[Category: Zhu P]] | ||
Current revision
In situ structure of polymerase complex of mammalian reovirus in the pre-elongation state
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