9hbr: Difference between revisions
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==TiLV-NP pentamer (pseudo-C5) (local refinement around 2 TiLV-NPs)== | |||
<StructureSection load='9hbr' size='340' side='right'caption='[[9hbr]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9hbr]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Tilapia_lake_virus Tilapia lake virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HBR 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P5P:PURINE+RIBOSIDE-5-MONOPHOSPHATE'>P5P</scene>, <scene name='pdbligand=Y5P:1-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-1,4-DIHYDROPYRIMIDINE'>Y5P</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=9hbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hbr OCA], [https://pdbe.org/9hbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hbr RCSB], [https://www.ebi.ac.uk/pdbsum/9hbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hbr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1Y9SHW7_9VIRU A0A1Y9SHW7_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tilapia Lake virus (TiLV) belongs to the Amnoonviridae family within the Articulavirales order of segmented negative-strand RNA viruses and is highly diverged from more familiar orthomyxoviruses, such as influenza. The viral nucleoprotein (NP), a key component of the replication machinery, packages the viral genome into protective ribonucleoprotein particles. Here we describe the electron cryo-microscopy (cryo-EM) structure of TiLV-NP bound to RNA within in vitro reconstituted, small ring-like, pseudo-symmetrical oligomers. Although TiLV-NP is considerably smaller than its influenza counterpart and unrelated in sequence, it maintains the same topology and domain organisation. This comprises a head and body domain between which is a positively charged groove, where single-stranded RNA binds. In addition, an oligomerisation loop inserts into a hydrophobic pocket in the neighbouring NP, the flexible hinges of which allow variable orientation of adjacent NPs. Focused cryo-EM maps unambiguously define the 5' to 3' direction of the bound RNA, confirmed by double stranded, A-form RNA regions that extrude out from some of the NP-NP interfaces. This is the first fully resolved description of how single-stranded and stem-loop RNA binds to an articulaviral NP assembly. Superposition with orthomyxoviral NPs suggest that the mode of RNA binding is likely similar across the Articulavirales order. | |||
Structure of the tilapia lake virus nucleoprotein bound to RNA.,Arragain B, Pelosse M, Huard K, Cusack S Nucleic Acids Res. 2025 Feb 8;53(4):gkaf112. doi: 10.1093/nar/gkaf112. PMID:39995042<ref>PMID:39995042</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9hbr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tilapia lake virus]] | |||
[[Category: Arragain B]] | |||
[[Category: Cusack S]] | |||
