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==Structure of SARS-CoV-2 Main Protease bound to 2,4'-Dimethylpropiophenone.== | ==Structure of SARS-CoV-2 Main Protease bound to 2,4'-Dimethylpropiophenone.== | ||
<StructureSection load='7adw' size='340' side='right'caption='[[7adw]]' scene=''> | <StructureSection load='7adw' size='340' side='right'caption='[[7adw]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ADW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7ADW FirstGlance]. <br> | <table><tr><td colspan='2'>[[7adw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ADW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7ADW FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7adw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7adw OCA], [http://pdbe.org/7adw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7adw RCSB], [http://www.ebi.ac.uk/pdbsum/7adw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7adw ProSAT]</span></td></tr> | </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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=R7Q:2-methyl-1-(4-methylphenyl)propan-1-one'>R7Q</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rep, 1a-1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7adw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7adw OCA], [http://pdbe.org/7adw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7adw RCSB], [http://www.ebi.ac.uk/pdbsum/7adw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7adw ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/R1AB_SARS2 R1AB_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] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7]<ref>PMID:32198291</ref> 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] Responsible for replication and transcription of the viral RNA genome.[UniProtKB:P0C6X7] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[UniProtKB:P0C6X7] Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.[UniProtKB:P0C6X7] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[UniProtKB:P0C6X7] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[UniProtKB:P0C6X7] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: 2019-ncov]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Awel, S]] | |||
[[Category: Awel S]] | [[Category: Beck, T]] | ||
[[Category: Beck T]] | [[Category: Betzel, C]] | ||
[[Category: Betzel C]] | [[Category: Brehm, W]] | ||
[[Category: Brehm W]] | [[Category: Brognaro, H]] | ||
[[Category: Brognaro H]] | [[Category: Chapman, H N]] | ||
[[Category: Chapman | [[Category: Chari, A]] | ||
[[Category: Chari A]] | [[Category: Domaracky, M]] | ||
[[Category: Domaracky M]] | [[Category: Doyle, J J]] | ||
[[Category: Doyle | [[Category: Dunkel, I]] | ||
[[Category: Dunkel I]] | [[Category: Ehrt, C]] | ||
[[Category: Ehrt C]] | [[Category: Ellinger, B]] | ||
[[Category: Ellinger B]] | [[Category: Esperanza, G Pena]] | ||
[[Category: Falke S]] | [[Category: Falke, S]] | ||
[[Category: Feiler C]] | [[Category: Feiler, C]] | ||
[[Category: | [[Category: Fischer, P]] | ||
[[Category: | [[Category: Fleckenstein, H]] | ||
[[Category: | [[Category: Franca, B Alves]] | ||
[[Category: Galchenkova M]] | [[Category: Galchenkova, M]] | ||
[[Category: Gelisio L]] | [[Category: Garcia, Y Fernandez]] | ||
[[Category: Gevorkov Y]] | [[Category: Gelisio, L]] | ||
[[Category: Ginn H]] | [[Category: Gevorkov, Y]] | ||
[[Category: Giseler H]] | [[Category: Ginn, H]] | ||
[[Category: Gribbon P]] | [[Category: Giseler, H]] | ||
[[Category: Groessler M]] | [[Category: Gribbon, P]] | ||
[[Category: Guenther S]] | [[Category: Groessler, M]] | ||
[[Category: Hakanpaeae J]] | [[Category: Guenther, S]] | ||
[[Category: Han H]] | [[Category: Hakanpaeae, J]] | ||
[[Category: Hennicke V]] | [[Category: Han, H]] | ||
[[Category: Hilgenfeld R]] | [[Category: Hennicke, V]] | ||
[[Category: Knoska J]] | [[Category: Hilgenfeld, R]] | ||
[[Category: Koua F]] | [[Category: Knoska, J]] | ||
[[Category: Kuzikov M]] | [[Category: Koua, F]] | ||
[[Category: Lane | [[Category: Kuzikov, M]] | ||
[[Category: Li C]] | [[Category: Lane, T J]] | ||
[[Category: Lieske J]] | [[Category: Li, C]] | ||
[[Category: Lorenzen K]] | [[Category: Lieske, J]] | ||
[[Category: Meents A]] | [[Category: Lorenzen, K]] | ||
[[Category: Mehrabi P]] | [[Category: Mashour, A Rahmani]] | ||
[[Category: Meier S]] | [[Category: Meents, A]] | ||
[[Category: Melo D]] | [[Category: Mehrabi, P]] | ||
[[Category: Meyer J]] | [[Category: Meier, S]] | ||
[[Category: Noei H]] | [[Category: Melo, D]] | ||
[[Category: Norton-Baker B]] | [[Category: Meyer, J]] | ||
[[Category: Oberthuer D]] | [[Category: Noei, H]] | ||
[[Category: Paulraj | [[Category: Norton-Baker, B]] | ||
[[Category: Pearson A]] | [[Category: Oberthuer, D]] | ||
[[Category: Peck A | [[Category: Paulraj, L X]] | ||
[[Category: Pearson, A]] | |||
[[Category: Perbandt M]] | [[Category: Peck, A]] | ||
[[Category: Pletzer-Zelgert J | [[Category: Perbandt, M]] | ||
[[Category: Pletzer-Zelgert, J]] | |||
[[Category: Rarey M]] | [[Category: Rarey, M]] | ||
[[Category: Reinke P]] | [[Category: Reinke, P]] | ||
[[Category: Saouane S]] | [[Category: Saouane, S]] | ||
[[Category: Schmidt C]] | [[Category: Schmidt, C]] | ||
[[Category: Schubert R]] | [[Category: Schubert, R]] | ||
[[Category: Schulz | [[Category: Schulz, E C]] | ||
[[Category: Schwinzer M]] | [[Category: Schwinzer, M]] | ||
[[Category: Seychell B]] | [[Category: Seychell, B]] | ||
[[Category: Tidow H]] | [[Category: Tidow, H]] | ||
[[Category: Tolstikova A]] | [[Category: Tolstikova, A]] | ||
[[Category: Trost F]] | [[Category: Trost, F]] | ||
[[Category: Turk D]] | [[Category: Turk, D]] | ||
[[Category: Ullah N]] | [[Category: Ullah, N]] | ||
[[Category: Weiss M]] | [[Category: Weiss, M]] | ||
[[Category: Werner N]] | [[Category: Werner, N]] | ||
[[Category: White | [[Category: White, T A]] | ||
[[Category: Wolf M]] | [[Category: Wolf, M]] | ||
[[Category: Wollenhaupt J]] | [[Category: Wollenhaupt, J]] | ||
[[Category: Yefanov O]] | [[Category: Yefanov, O]] | ||
[[Category: Zaliani A]] | [[Category: Zaliani, A]] | ||
[[Category: Zhang L]] | [[Category: Zhang, L]] | ||
[[Category: Covid-19]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mpro]] | |||
[[Category: Peptide binding protein]] | |||
[[Category: Sars-cov-2]] | |||