View source for 7yes


==The structure of EBOV L-VP35-RNA complex (state2)==
<StructureSection load='7yes' size='340' side='right'caption='[[7yes]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7yes]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebola_virus Ebola virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YES 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]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7yes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yes OCA], [https://pdbe.org/7yes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yes RCSB], [https://www.ebi.ac.uk/pdbsum/7yes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yes ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1C4HDK9_9MONO A0A1C4HDK9_9MONO] Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling.[PIRNR:PIRNR018326]
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== Publication Abstract from PubMed ==
Filoviruses, including Ebola virus, pose an increasing threat to the public health. Although two therapeutic monoclonal antibodies have been approved to treat the Ebola virus disease(1,2), there are no approved broadly reactive drugs to control diverse filovirus infection. Filovirus has a large polymerase (L) protein and the cofactor viral protein 35 (VP35), which constitute the basic functional unit responsible for virus genome RNA synthesis(3). Owing to its conservation, the L-VP35 polymerase complex is a promising target for broadly reactive antiviral drugs. Here we determined the structure of Ebola virus L protein in complex with tetrameric VP35 using cryo-electron microscopy (state 1). Structural analysis revealed that Ebola virus L possesses a filovirus-specific insertion element that is essential for RNA synthesis, and that VP35 interacts extensively with the N-terminal region of L by three protomers of the VP35 tetramer. Notably, we captured the complex structure in a second conformation with the unambiguous priming loop and supporting helix away from polymerase active site (state 2). Moreover, we demonstrated that the century-old drug suramin could inhibit the activity of the Ebola virus polymerase in an enzymatic assay. The structure of the L-VP35-suramin complex reveals that suramin can bind at the highly conserved NTP entry channel to prevent substrates from entering the active site. These findings reveal the mechanism of Ebola virus replication and may guide the development of more powerful anti-filovirus drugs.

Structure of the Ebola virus polymerase complex.,Yuan B, Peng Q, Cheng J, Wang M, Zhong J, Qi J, Gao GF, Shi Y Nature. 2022 Oct;610(7931):394-401. doi: 10.1038/s41586-022-05271-2. Epub 2022 , Sep 28. PMID:36171293<ref>PMID:36171293</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 7yes" style="background-color:#fffaf0;"></div>

==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Ebola virus]]
[[Category: Large Structures]]
[[Category: Peng Q]]
[[Category: Shi Y]]
[[Category: Yuan B]]