7ofu: Difference between revisions

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<StructureSection load='7ofu' size='340' side='right'caption='[[7ofu]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='7ofu' size='340' side='right'caption='[[7ofu]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7nfv|7nfv]], [[7ofs|7ofs]], [[7oft|7oft]]</div></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ofu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofu OCA], [https://pdbe.org/7ofu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofu RCSB], [https://www.ebi.ac.uk/pdbsum/7ofu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofu ProSAT]</span></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=7ofu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofu OCA], [https://pdbe.org/7ofu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofu RCSB], [https://www.ebi.ac.uk/pdbsum/7ofu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofu ProSAT]</span></td></tr>
</table>
</table>
== 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]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 2019-ncov]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Andaleeb, H]]
[[Category: Alves Franca B]]
[[Category: Awel, S]]
[[Category: Andaleeb H]]
[[Category: Betzel, C]]
[[Category: Awel S]]
[[Category: Brings, L]]
[[Category: Betzel C]]
[[Category: Brognaro, H]]
[[Category: Brings L]]
[[Category: Chapman, H N]]
[[Category: Brognaro H]]
[[Category: Choudary, I]]
[[Category: Chapman HN]]
[[Category: Ewert, W]]
[[Category: Choudary I]]
[[Category: Falke, S]]
[[Category: Ewert W]]
[[Category: Fleckenstein, H]]
[[Category: Falke S]]
[[Category: Franca, B Alves]]
[[Category: Fleckenstein H]]
[[Category: Galchenkova, M]]
[[Category: Galchenkova M]]
[[Category: Gelisio, L]]
[[Category: Gelisio L]]
[[Category: Gevorkov, Y]]
[[Category: Gevorkov Y]]
[[Category: Ginn, H]]
[[Category: Ginn H]]
[[Category: Groessler, M]]
[[Category: Groessler M]]
[[Category: Guenther, S]]
[[Category: Guenther S]]
[[Category: Hakanpaeae, J]]
[[Category: Hakanpaeae J]]
[[Category: Han, H]]
[[Category: Han H]]
[[Category: Hinrichs, W]]
[[Category: Hinrichs W]]
[[Category: Koua, F]]
[[Category: Koua F]]
[[Category: Lane, T J]]
[[Category: Lane TJ]]
[[Category: Li, C]]
[[Category: Li C]]
[[Category: Lieske, J]]
[[Category: Lieske J]]
[[Category: Lorenzen, K]]
[[Category: Lorenzen K]]
[[Category: Meents, A]]
[[Category: Meents A]]
[[Category: Perbandt, M]]
[[Category: Perbandt M]]
[[Category: Perk, A]]
[[Category: Perk A]]
[[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: Schwinzer, M]]
[[Category: Schwinzer M]]
[[Category: Sprenger, J]]
[[Category: Sprenger J]]
[[Category: Srinivasan, V]]
[[Category: Srinivasan V]]
[[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: Wahab, A]]
[[Category: Wahab A]]
[[Category: Wang, M]]
[[Category: Wang M]]
[[Category: Werner, N]]
[[Category: Werner N]]
[[Category: Wolf, M]]
[[Category: Wolf M]]
[[Category: Yefanov, O]]
[[Category: Yefanov O]]
[[Category: Hydrolase]]
[[Category: Papain-like protease sars-cov-2 hydrolase zinc binding protein]]

Latest revision as of 08:01, 18 September 2024

Structure of SARS-CoV-2 Papain-like protease PLpro in complex with 3, 4-Dihydroxybenzoic acid, methyl esterStructure of SARS-CoV-2 Papain-like protease PLpro in complex with 3, 4-Dihydroxybenzoic acid, methyl ester

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.72Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7ofu, resolution 1.72Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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