9p0f

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m (Protected "9p0f" [edit=sysop:move=sysop])
Current revision (06:25, 25 June 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9p0f is ON HOLD
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==Crystal Structure of the C-terminal Cytoplasmic Domain of nsp4 from SARS-CoV-2==
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<StructureSection load='9p0f' size='340' side='right'caption='[[9p0f]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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Authors: Minasov, G., Shuvalova, L., Brunzelle, J.S., Satchell, K.J.F., Center for Structural Biology of Infectious Diseases (CSBID)
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9p0f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9P0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9P0F FirstGlance]. <br>
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Description: Crystal Structure of the C-terminal Cytoplasmic Domain of nsp4 from SARS-CoV-2
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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[[Category: Satchell, K.J.F]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9p0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9p0f OCA], [https://pdbe.org/9p0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9p0f RCSB], [https://www.ebi.ac.uk/pdbsum/9p0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9p0f ProSAT]</span></td></tr>
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[[Category: Shuvalova, L]]
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</table>
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[[Category: Minasov, G]]
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== Function ==
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[[Category: Brunzelle, J.S]]
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[https://www.uniprot.org/uniprot/R1A_SARS2 R1A_SARS2] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7]
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[[Category: Center For Structural Biology Of Infectious Diseases (Csbid)]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Severe acute respiratory syndrome coronavirus 2]]
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[[Category: Brunzelle JS]]
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[[Category: Minasov G]]
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[[Category: Satchell KJF]]
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[[Category: Shuvalova L]]

Current revision

Crystal Structure of the C-terminal Cytoplasmic Domain of nsp4 from SARS-CoV-2

PDB ID 9p0f

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