View source for 8asb


==Structure of the SFTSV L protein stalled at early elongation with the endonuclease domain in a raised conformation [EARLY-ELONGATION-ENDO]==
<StructureSection load='8asb' size='340' side='right'caption='[[8asb]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8asb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/SFTS_virus_AH12 SFTS virus AH12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ASB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ASB 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]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2KH:5-O-[(S)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]URIDINE'>2KH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8asb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8asb OCA], [https://pdbe.org/8asb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8asb RCSB], [https://www.ebi.ac.uk/pdbsum/8asb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8asb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U3GU88_SFTS U3GU88_SFTS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Severe fever with thrombocytopenia syndrome virus (SFTSV) is a phenuivirus that has rapidly become endemic in several East Asian countries. The large (L) protein of SFTSV, which includes the RNA-dependent RNA polymerase (RdRp), is responsible for catalysing viral genome replication and transcription. Here, we present 5 cryo-electron microscopy (cryo-EM) structures of the L protein in several states of the genome replication process, from pre-initiation to late-stage elongation, at a resolution of up to 2.6 A. We identify how the L protein binds the 5' viral RNA in a hook-like conformation and show how the distal 5' and 3' RNA ends form a duplex positioning the 3' RNA terminus in the RdRp active site ready for initiation. We also observe the L protein stalled in the early and late stages of elongation with the RdRp core accommodating a 10-bp product-template duplex. This duplex ultimately splits with the template binding to a designated 3' secondary binding site. The structural data and observations are complemented by in vitro biochemical and cell-based mini-replicon assays. Altogether, our data provide novel key insights into the mechanism of viral genome replication by the SFTSV L protein and will aid drug development against segmented negative-strand RNA viruses.

Structural insights into viral genome replication by the severe fever with thrombocytopenia syndrome virus L protein.,Williams HM, Thorkelsson SR, Vogel D, Milewski M, Busch C, Cusack S, Grunewald K, Quemin ERJ, Rosenthal M Nucleic Acids Res. 2023 Feb 22;51(3):1424-1442. doi: 10.1093/nar/gkac1249. PMID:36651274<ref>PMID:36651274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8asb" style="background-color:#fffaf0;"></div>

==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: SFTS virus AH12]]
[[Category: Busch C]]
[[Category: Cusack S]]
[[Category: Grunewald K]]
[[Category: Milewski M]]
[[Category: Quemin ERJ]]
[[Category: Rosenthal M]]
[[Category: Thorkelsson SR]]
[[Category: Vogel D]]
[[Category: Williams HM]]