View source for 6kur


==Structure of influenza D virus polymerase bound to vRNA promoter in Mode B conformation (Class B1)==
<SX load='6kur' size='340' side='right' viewer='molstar' caption='[[6kur]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kur]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_D_virus_(D/swine/Oklahoma/1334/2011) Influenza D virus (D/swine/Oklahoma/1334/2011)] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KUR 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]] 3.7&#8491;</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=6kur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kur OCA], [https://pdbe.org/6kur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kur RCSB], [https://www.ebi.ac.uk/pdbsum/6kur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kur ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K9LHF3_9ORTO K9LHF3_9ORTO] 
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== Publication Abstract from PubMed ==
The influenza virus polymerase uses capped RNA primers to initiate transcription, and a combination of terminal and internal de novo initiations for the two-step replication process by binding the conserved viral genomic RNA (vRNA) or complementary RNA (cRNA) promoter. Here, we determined the apo and promoter-bound influenza D polymerase structures using cryo-electron microscopy and found the polymerase has an evolutionarily conserved stable core structure with inherently flexible peripheral domains. Strikingly, two conformations (mode A and B) of the vRNA promoter were observed where the 3'-vRNA end can bind at two different sites, whereas the cRNA promoter only binds in the mode B conformation. Functional studies confirmed the critical role of the mode B conformation for vRNA synthesis via the intermediate cRNA but not for cRNA production, which is mainly regulated by the mode A conformation. Both conformations participate in the regulation of the transcription process. This work advances our understanding of the regulatory mechanisms for the synthesis of different RNA species by influenza virus polymerase and opens new opportunities for antiviral drug design.

Structural insight into RNA synthesis by influenza D polymerase.,Peng Q, Liu Y, Peng R, Wang M, Yang W, Song H, Chen Y, Liu S, Han M, Zhang X, Wang P, Yan J, Zhang B, Qi J, Deng T, Gao GF, Shi Y Nat Microbiol. 2019 Jun 17. pii: 10.1038/s41564-019-0487-5. doi:, 10.1038/s41564-019-0487-5. PMID:31209309<ref>PMID:31209309</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6kur" style="background-color:#fffaf0;"></div>

==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Gao GF]]
[[Category: Peng Q]]
[[Category: Peng R]]
[[Category: Qi J]]
[[Category: Shi Y]]