View source for 7yed


==In situ structure of polymerase complex of mammalian reovirus in the elongation state==
<StructureSection load='7yed' size='340' side='right'caption='[[7yed]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yed]] is a 25 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=7YED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YED 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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=7yed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yed OCA], [https://pdbe.org/7yed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yed RCSB], [https://www.ebi.ac.uk/pdbsum/7yed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yed ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9E874_9REOV C9E874_9REOV] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7yed" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mammalian orthoreovirus 3]]
[[Category: Bao KY]]
[[Category: Li DY]]
[[Category: Zhang XL]]
[[Category: Zhu P]]