6t2c: Difference between revisions
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==Bat Influenza A polymerase recycling complex== | ==Bat Influenza A polymerase recycling complex== | ||
<StructureSection load='6t2c' size='340' side='right'caption='[[6t2c]]' scene=''> | <StructureSection load='6t2c' size='340' side='right'caption='[[6t2c]], [[Resolution|resolution]] 3.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T2C OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6t2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/little_yellow-shouldered_bat/Guatemala/060/2010(H17N10)) Influenza A virus (A/little yellow-shouldered bat/Guatemala/060/2010(H17N10))] and [https://en.wikipedia.org/wiki/Influenza_B_virus Influenza B virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T2C FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.52Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6t2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t2c OCA], [https://pdbe.org/6t2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t2c RCSB], [https://www.ebi.ac.uk/pdbsum/6t2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t2c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H6QM90_9INFA H6QM90_9INFA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Influenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP. | |||
A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase.,Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S Cell. 2020 Apr 16. pii: S0092-8674(20)30389-5. doi: 10.1016/j.cell.2020.03.061. PMID:32304664<ref>PMID:32304664</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6t2c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Influenza B virus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cusack S]] | [[Category: Cusack S]] | ||
[[Category: Kouba T]] | [[Category: Kouba T]] | ||
[[Category: Wandzik JM]] | [[Category: Wandzik JM]] | ||
Latest revision as of 13:17, 22 May 2024
Bat Influenza A polymerase recycling complexBat Influenza A polymerase recycling complex
Structural highlights
FunctionPublication Abstract from PubMedInfluenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP. A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase.,Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S Cell. 2020 Apr 16. pii: S0092-8674(20)30389-5. doi: 10.1016/j.cell.2020.03.061. PMID:32304664[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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