6rid: Difference between revisions

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-'''Unreleased structure'''
-The entry 6rid is ON HOLD
+==Structure of Vaccinia Virus DNA-dependent RNA polymerase elongation complex==
+<SX load='6rid' size='340' side='right' viewer='molstar' caption='[[6rid]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6rid]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] and [https://en.wikipedia.org/wiki/Vaccinia_virus_GLV-1h68 Vaccinia virus GLV-1h68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RID 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]] 2.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6rid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rid OCA], [https://pdbe.org/6rid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rid RCSB], [https://www.ebi.ac.uk/pdbsum/6rid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rid ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate m(7)G-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA.
-Authors:
+Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.,Hillen HS, Bartuli J, Grimm C, Dienemann C, Bedenk K, Szalay AA, Fischer U, Cramer P Cell. 2019 Dec 12;179(7):1525-1536.e12. doi: 10.1016/j.cell.2019.11.023. PMID:31835031<ref>PMID:31835031</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6rid" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Large Structures]]
+[[Category: Vaccinia virus]]
+[[Category: Vaccinia virus GLV-1h68]]
+[[Category: Bartuli J]]
+[[Category: Bedenk K]]
+[[Category: Cramer P]]
+[[Category: Dienemann C]]
+[[Category: Fischer U]]
+[[Category: Grimm C]]
+[[Category: Hillen HS]]
+[[Category: Szalar A]]