4cbg
From Proteopedia
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==Pestivirus NS3 helicase== | ==Pestivirus NS3 helicase== | ||
| - | <StructureSection load='4cbg' size='340' side='right' caption='[[4cbg]], [[Resolution|resolution]] 2.82Å' scene=''> | + | <StructureSection load='4cbg' size='340' side='right'caption='[[4cbg]], [[Resolution|resolution]] 2.82Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4cbg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBG OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4cbg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Classical_swine_fever_virus Classical swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.82Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4cbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbg OCA], [https://pdbe.org/4cbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbg RCSB], [https://www.ebi.ac.uk/pdbsum/4cbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbg ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/POLG_CSFAT POLG_CSFAT] Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.<ref>PMID:17215286</ref> <ref>PMID:19540847</ref> <ref>PMID:24606708</ref> <ref>PMID:27334592</ref> Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Also plays a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.<ref>PMID:28290554</ref> <ref>PMID:9617770</ref> Plays a role in viral entry. Interacts with host RPSA that acts as a cellular attachment receptor for the virus. Possesses also intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections. Cleaves preferentially NpU bonds (PubMed:15113930).<ref>PMID:15113930</ref> <ref>PMID:19264773</ref> <ref>PMID:19767841</ref> <ref>PMID:25694590</ref> <ref>PMID:29235980</ref> <ref>PMID:8356450</ref> Plays a role in cell attachment and subsequent fusion of viral and cellular membranes. Therefore, mediates together with envelope glycoprotein E2 the viral entry.<ref>PMID:15527858</ref> Plays a role in cell attachment and subsequent fusion of viral and cellular membranes (PubMed:15527858). Therefore, mediates together with envelope glycoprotein E1 the viral entry (PubMed:15527858). Binds to host ADAM17 receptor for entry (PubMed:33684175).<ref>PMID:15527858</ref> <ref>PMID:33684175</ref> Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules.<ref>PMID:22496228</ref> <ref>PMID:24189547</ref> Autoprotease that associates with the host chaperone JIV and cleaves the NS2-3 protein between NS2 and NS3. Also plays a role in the formation of infectious particles.<ref>PMID:17482232</ref> Plays a role in the regulation of viral RNA replication.<ref>PMID:10438869</ref> Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in the inhibition of host NF-kappa-B activation by interacting with and inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.<ref>PMID:19185595</ref> <ref>PMID:28751780</ref> Acts as a cofactor for the NS3 protease activity.<ref>PMID:17482232</ref> Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Antagonizes host cell apoptosis by interacting with host ferritin heavy chain. The ORF4 protein physically binds host FTH1/FHC, resulting in the reduction of FTH1 protein levels in host cells. Reduction of FTH1 concentration further inhibits the accumulation of reactive oxygen in host cells, leading to reduced apoptosis (By similarity) (PubMed:29844394).[UniProtKB:O56125][UniProtKB:Q9Q6P4]<ref>PMID:29844394</ref> Regulates viral RNA replication by interacting with the 3'-untranslated region of viral RNA in a dose-dependent manner. At small concentrations promotes viral synthesis by interacting with the polymerase NS5B while at large concentrations, inhibits replication.<ref>PMID:22261205</ref> <ref>PMID:22795973</ref> Replicates the viral (+) and (-) genome.[PROSITE-ProRule:PRU00539] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4cbg" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Helicase 3D structures|Helicase 3D structures]] | ||
| + | *[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bricogne | + | [[Category: Classical swine fever virus]] |
| - | [[Category: Duquerroy | + | [[Category: Large Structures]] |
| - | [[Category: Kwok | + | [[Category: Bricogne G]] |
| - | [[Category: Lamp | + | [[Category: Duquerroy S]] |
| - | [[Category: Perez | + | [[Category: Kwok J]] |
| - | [[Category: Rey | + | [[Category: Lamp B]] |
| - | [[Category: Rumenapf | + | [[Category: Perez J]] |
| - | [[Category: Tortorici | + | [[Category: Rey FA]] |
| - | [[Category: Vachette | + | [[Category: Rumenapf T]] |
| - | [[Category: Vonrhein | + | [[Category: Tortorici MA]] |
| - | + | [[Category: Vachette P]] | |
| - | + | [[Category: Vonrhein C]] | |
| - | + | ||
Current revision
Pestivirus NS3 helicase
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