7orn: Difference between revisions
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==La Crosse virus polymerase at replication initiation stage== | |||
<StructureSection load='7orn' size='340' side='right'caption='[[7orn]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7orn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Orthobunyavirus_lacrosseense Orthobunyavirus lacrosseense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORN 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=7orn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7orn OCA], [https://pdbe.org/7orn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7orn RCSB], [https://www.ebi.ac.uk/pdbsum/7orn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7orn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/L_BUNLC L_BUNLC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Segmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse virus polymerase and visualize its conformational dynamics by cryo-electron microscopy, unveiling the precise molecular mechanics underlying its essential activities. We find that replication initiation is coupled to distal duplex promoter formation, endonuclease movement, prime-and-realign loop extension and closure of the polymerase core that direct the template towards the active site. Transcription initiation depends on C-terminal region closure and endonuclease movements that prompt primer cleavage prior to primer entry in the active site. Product realignment after priming, observed in replication and transcription, is triggered by the prime-and-realign loop. Switch to elongation results in polymerase reorganization and core region opening to facilitate template-product duplex formation in the active site cavity. The uncovered detailed mechanics should be helpful for the future design of antivirals counteracting bunyaviral life threatening pathogens. | |||
Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription.,Arragain B, Durieux Trouilleton Q, Baudin F, Provaznik J, Azevedo N, Cusack S, Schoehn G, Malet H Nat Commun. 2022 Feb 16;13(1):902. doi: 10.1038/s41467-022-28428-z. PMID:35173159<ref>PMID:35173159</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7orn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Orthobunyavirus lacrosseense]] | |||
[[Category: Arragain B]] | |||
[[Category: Baudin F]] | |||
[[Category: Cusack S]] | |||
[[Category: Durieux Trouilleton Q]] | |||
[[Category: Malet H]] | |||
[[Category: Schoehn G]] | |||
Latest revision as of 15:28, 17 July 2024
La Crosse virus polymerase at replication initiation stageLa Crosse virus polymerase at replication initiation stage
Structural highlights
FunctionPublication Abstract from PubMedSegmented negative-strand RNA bunyaviruses encode a multi-functional polymerase that performs genome replication and transcription. Here, we establish conditions for in vitro activity of La Crosse virus polymerase and visualize its conformational dynamics by cryo-electron microscopy, unveiling the precise molecular mechanics underlying its essential activities. We find that replication initiation is coupled to distal duplex promoter formation, endonuclease movement, prime-and-realign loop extension and closure of the polymerase core that direct the template towards the active site. Transcription initiation depends on C-terminal region closure and endonuclease movements that prompt primer cleavage prior to primer entry in the active site. Product realignment after priming, observed in replication and transcription, is triggered by the prime-and-realign loop. Switch to elongation results in polymerase reorganization and core region opening to facilitate template-product duplex formation in the active site cavity. The uncovered detailed mechanics should be helpful for the future design of antivirals counteracting bunyaviral life threatening pathogens. Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription.,Arragain B, Durieux Trouilleton Q, Baudin F, Provaznik J, Azevedo N, Cusack S, Schoehn G, Malet H Nat Commun. 2022 Feb 16;13(1):902. doi: 10.1038/s41467-022-28428-z. PMID:35173159[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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