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| | <StructureSection load='6vag' size='340' side='right'caption='[[6vag]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='6vag' size='340' side='right'caption='[[6vag]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vag]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Piv5 Piv5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VAG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vag]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_virus_5_(strain_W3) Simian virus 5 (strain W3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VAG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P/V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11208 PIV5])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vag OCA], [http://pdbe.org/6vag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vag RCSB], [http://www.ebi.ac.uk/pdbsum/6vag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vag ProSAT]</span></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=6vag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vag OCA], [https://pdbe.org/6vag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vag RCSB], [https://www.ebi.ac.uk/pdbsum/6vag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vag ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/PHOSP_PIV5 PHOSP_PIV5] |
| - | Paramyxoviruses are enveloped, nonsegmented, negative-strand RNA viruses that cause a wide spectrum of human and animal diseases. The viral genome, packaged by the nucleoprotein (N), serves as a template for the polymerase complex, composed of the large protein (L) and the homo-tetrameric phosphoprotein (P). The approximately 250-kDa L possesses all enzymatic activities necessary for its function but requires P in vivo. Structural information is available for individual P domains from different paramyxoviruses, but how P interacts with L and how that affects the activity of L is largely unknown due to the lack of high-resolution structures of this complex in this viral family. In this study we determined the structure of the L-P complex from parainfluenza virus 5 (PIV5) at 4.3-A resolution using cryoelectron microscopy, as well as the oligomerization domain (OD) of P at 1.4-A resolution using X-ray crystallography. P-OD associates with the RNA-dependent RNA polymerase domain of L and protrudes away from it, while the X domain of one chain of P is bound near the L nucleotide entry site. The methyltransferase (MTase) domain and the C-terminal domain (CTD) of L adopt a unique conformation, positioning the MTase active site immediately above the poly-ribonucleotidyltransferase domain and near the likely exit site for the product RNA 5' end. Our study reveals a potential mechanism that mononegavirus polymerases may employ to switch between transcription and genome replication. This knowledge will assist in the design and development of antivirals against paramyxoviruses.
| + | |
| - | | + | |
| - | Structure of a paramyxovirus polymerase complex reveals a unique methyltransferase-CTD conformation.,Abdella R, Aggarwal M, Okura T, Lamb RA, He Y Proc Natl Acad Sci U S A. 2020 Feb 19. pii: 1919837117. doi:, 10.1073/pnas.1919837117. PMID:32075920<ref>PMID:32075920</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6vag" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Piv5]]
| + | [[Category: Abdella R]] |
| - | [[Category: Abdella, R]] | + | [[Category: Aggarwal M]] |
| - | [[Category: Aggarwal, M]] | + | [[Category: He Y]] |
| - | [[Category: He, Y]] | + | [[Category: Lamb RA]] |
| - | [[Category: Lamb, R A]] | + | |
| - | [[Category: Oligomerization domain]]
| + | |
| - | [[Category: Paramyxovirus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
