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==Crystal structure of Reston ebolavirus VP35 RNA binding domain==
==Crystal structure of Reston ebolavirus VP35 RNA binding domain==
<StructureSection load='3ks4' size='340' side='right' caption='[[3ks4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3ks4' size='340' side='right'caption='[[3ks4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ks4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebore Ebore]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KS4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ks4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Reston_ebolavirus_-_Reston Reston ebolavirus - Reston]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KS4 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fke|3fke]], [[3ks8|3ks8]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">REBOVgp2, VP35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=129003 EBORE])</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=3ks4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ks4 OCA], [https://pdbe.org/3ks4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ks4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ks4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ks4 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ks4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ks4 OCA], [http://pdbe.org/3ks4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ks4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ks4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ks4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VP35_EBORR VP35_EBORR]] Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. The mechanism by which this blockage occurs remains incompletely defined, a hypothesis suggests that VP35 dsRNA-binding activity prevents activation of IRF3 by sequestering dsRNA. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity).  
[https://www.uniprot.org/uniprot/VP35_EBORR VP35_EBORR] Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. The mechanism by which this blockage occurs remains incompletely defined, a hypothesis suggests that VP35 dsRNA-binding activity prevents activation of IRF3 by sequestering dsRNA. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ks4 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ks4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ebolavirus causes a severe hemorrhagic fever and is divided into five distinct species, of which Reston ebolavirus is uniquely nonpathogenic to humans. Disease caused by ebolavirus is marked by early immunosuppression of innate immune signaling events, involving silencing and sequestration of double-stranded RNA (dsRNA) by the viral protein VP35. Here we present unbound and dsRNA-bound crystal structures of the dsRNA-binding domain of Reston ebolavirus VP35. The structures show that VP35 forms an unusual, asymmetric dimer on dsRNA binding, with each of the monomers binding dsRNA in a different way: one binds the backbone whereas the other caps the terminus. Additional SAXS, DXMS, and dsRNA-binding experiments presented here support a model of cooperative dsRNA recognition in which binding of the first monomer assists binding of the next monomer of the oligomeric VP35 protein. This work illustrates how ebolavirus VP35 could mask key recognition sites of molecules such as RIG-I, MDA-5, and Dicer to silence viral dsRNA in infection.
Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression.,Kimberlin CR, Bornholdt ZA, Li S, Woods VL Jr, Macrae IJ, Saphire EO Proc Natl Acad Sci U S A. 2009 Dec 14. PMID:20018665<ref>PMID:20018665</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ks4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ebore]]
[[Category: Large Structures]]
[[Category: Bornholdt, Z A]]
[[Category: Reston ebolavirus - Reston]]
[[Category: Kimberlin, C R]]
[[Category: Bornholdt ZA]]
[[Category: Li, S]]
[[Category: Kimberlin CR]]
[[Category: Macrae, I J]]
[[Category: Li S]]
[[Category: Saphire, E O]]
[[Category: Macrae IJ]]
[[Category: Woods, V L]]
[[Category: Saphire EO]]
[[Category: Ebolavirus]]
[[Category: Woods VL]]
[[Category: Host cytoplasm]]
[[Category: Interferon]]
[[Category: Interferon antiviral system evasion]]
[[Category: Protein-rna complex]]
[[Category: Reston]]
[[Category: Rna binding protein]]
[[Category: Rna replication]]
[[Category: Rna-binding]]
[[Category: Rna-binding protein]]
[[Category: Transcription]]
[[Category: Viral protein]]
[[Category: Virion]]

Latest revision as of 10:18, 21 February 2024

Crystal structure of Reston ebolavirus VP35 RNA binding domain

3ks4, resolution 2.40Å

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