7ofu

<table><tr><td colspan='2'>[[7ofu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OFU FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HE9:methyl+3,4-bis(oxidanyl)benzoate'>HE9</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

== Function ==

[[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]

[[Category: 2019-ncov]]

[[Category: Andaleeb, H]]

[[Category: Awel, S]]

[[Category: Betzel, C]]

[[Category: Brings, L]]

[[Category: Brognaro, H]]

[[Category: Chapman, H N]]

[[Category: Choudary, I]]

[[Category: Ewert, W]]

[[Category: Falke, S]]

[[Category: Fleckenstein, H]]

[[Category: Franca, B Alves]]

[[Category: Galchenkova, M]]

[[Category: Gelisio, L]]

[[Category: Gevorkov, Y]]

[[Category: Ginn, H]]

[[Category: Groessler, M]]

[[Category: Guenther, S]]

[[Category: Hakanpaeae, J]]

[[Category: Han, H]]

[[Category: Hinrichs, W]]

[[Category: Koua, F]]

[[Category: Lane, T J]]

[[Category: Li, C]]

[[Category: Lieske, J]]

[[Category: Lorenzen, K]]

[[Category: Meents, A]]

[[Category: Perbandt, M]]

[[Category: Perk, A]]

[[Category: Reinke, P]]

[[Category: Saouane, S]]

[[Category: Schmidt, C]]

[[Category: Schubert, R]]

[[Category: Schwinzer, M]]

[[Category: Sprenger, J]]

[[Category: Srinivasan, V]]

[[Category: Tolstikova, A]]

[[Category: Trost, F]]

[[Category: Turk, D]]

[[Category: Ullah, N]]

[[Category: Wahab, A]]

[[Category: Wang, M]]

[[Category: Werner, N]]

[[Category: Wolf, M]]

[[Category: Yefanov, O]]

[[Category: Hydrolase papain-like protease plpro complex]]