7yot: Difference between revisions

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-'''Unreleased structure'''
-The entry 7yot is ON HOLD  until Paper Publication
+==Cryo-EM structure of RNA polymerase in complex with P protein tetramer of Newcastle disease virus==
+<StructureSection load='7yot' size='340' side='right'caption='[[7yot]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7yot]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_orthoavulavirus_1 Avian orthoavulavirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YOT 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yot OCA], [https://pdbe.org/7yot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yot RCSB], [https://www.ebi.ac.uk/pdbsum/7yot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yot ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0S2UXI9_9MONO A0A0S2UXI9_9MONO]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Newcastle disease virus (NDV) belongs to Paramyxoviridae, which contains lethal human and animal pathogens. NDV RNA genome is replicated and transcribed by a multifunctional 250 kDa RNA-dependent RNA polymerase (L protein). To date, high-resolution structure of NDV L protein complexed with P protein remains to be elucidated, limiting our understanding of the molecular mechanisms of Paramyxoviridae replication/transcription. Here, we used cryo-EM and enzymatic assays to investigate the structure-function relationship of L-P complex. We found that C-terminal of CD-MTase-CTD module of the atomic-resolution L-P complex conformationally rearranges, and the priming/intrusion loops are likely in RNA elongation conformations different from previous structures. The P protein adopts a unique tetrameric organization and interacts with L protein. Our findings indicate that NDV L-P complex represents elongation state distinct from previous structures. Our work greatly advances the understanding of Paramyxoviridae RNA synthesis, revealing how initiation/elongation alternates, providing clues for identifying therapeutic targets against Paramyxoviridae.
-Authors:
+Structure of the Newcastle Disease Virus L protein in complex with tetrameric phosphoprotein.,Cong J, Feng X, Kang H, Fu W, Wang L, Wang C, Li X, Chen Y, Rao Z Nat Commun. 2023 Mar 10;14(1):1324. doi: 10.1038/s41467-023-37012-y. PMID:36898997<ref>PMID:36898997</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 7yot" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Avian orthoavulavirus 1]]
+[[Category: Large Structures]]
+[[Category: Chen Y]]
+[[Category: Jingyuan C]]