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| | <StructureSection load='5bz0' size='340' side='right'caption='[[5bz0]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5bz0' size='340' side='right'caption='[[5bz0]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bz0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Avian_infectious_bronchitis_virus_(strain_beaudette) Avian infectious bronchitis virus (strain beaudette)] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BZ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bz0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_infectious_bronchitis_virus_(strain_Beaudette) Avian infectious bronchitis virus (strain Beaudette)] and [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BZ0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=11122 Avian infectious bronchitis virus (strain Beaudette)])</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=5bz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bz0 OCA], [https://pdbe.org/5bz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bz0 RCSB], [https://www.ebi.ac.uk/pdbsum/5bz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bz0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bz0 OCA], [http://pdbe.org/5bz0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bz0 RCSB], [http://www.ebi.ac.uk/pdbsum/5bz0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bz0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/R1AB_IBVB R1AB_IBVB]] The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:11413307</ref> The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. Activity of PL-PRO is dependent on zinc (By similarity).<ref>PMID:11413307</ref> The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity).<ref>PMID:11413307</ref> The peptide p16 might be involved in the EGF signaling pathway.<ref>PMID:11413307</ref> The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).<ref>PMID:11413307</ref> The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction (By similarity).<ref>PMID:11413307</ref> Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).<ref>PMID:11413307</ref> Nsp9 is a ssRNA-binding protein (By similarity).<ref>PMID:11413307</ref> NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond (By similarity).<ref>PMID:11413307</ref> [[http://www.uniprot.org/uniprot/RS27A_BOVIN RS27A_BOVIN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). Ribosomal protein S27a is a component of the 40S subunit of the ribosome. | + | [https://www.uniprot.org/uniprot/R1AB_IBVB R1AB_IBVB] The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:11413307</ref> The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. Activity of PL-PRO is dependent on zinc (By similarity).<ref>PMID:11413307</ref> The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity).<ref>PMID:11413307</ref> The peptide p16 might be involved in the EGF signaling pathway.<ref>PMID:11413307</ref> The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).<ref>PMID:11413307</ref> The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction (By similarity).<ref>PMID:11413307</ref> Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).<ref>PMID:11413307</ref> Nsp9 is a ssRNA-binding protein (By similarity).<ref>PMID:11413307</ref> NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond (By similarity).<ref>PMID:11413307</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kong, L Y]] | + | [[Category: Kong LY]] |
| - | [[Category: Rao, Z H]] | + | [[Category: Rao ZH]] |
| - | [[Category: Yan, L M]] | + | [[Category: Yan LM]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Dub]]
| + | |
| - | [[Category: Hydrolase-protein binding complex]]
| + | |
| - | [[Category: Ibv]]
| + | |
| - | [[Category: Papain-like protease]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| Structural highlights
Function
R1AB_IBVB The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.[1] The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. Activity of PL-PRO is dependent on zinc (By similarity).[2] The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK (By similarity).[3] The peptide p16 might be involved in the EGF signaling pathway.[4] The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).[5] The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction (By similarity).[6] Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).[7] Nsp9 is a ssRNA-binding protein (By similarity).[8] NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond (By similarity).[9]
References
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
- ↑ Liu C, Xu HY, Liu DX. Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus. J Virol. 2001 Jul;75(14):6402-9. PMID:11413307 doi:http://dx.doi.org/10.1128/JVI.75.14.6402-6409.2001
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