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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[7z2j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/White_bream_virus White bream virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z2J FirstGlance]. <br> | | <table><tr><td colspan='2'>[[7z2j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/White_bream_virus White bream virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z2J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 1.657Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7z2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z2j OCA], [https://pdbe.org/7z2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z2j RCSB], [https://www.ebi.ac.uk/pdbsum/7z2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z2j 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=7z2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z2j OCA], [https://pdbe.org/7z2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z2j RCSB], [https://www.ebi.ac.uk/pdbsum/7z2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z2j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [https://www.uniprot.org/uniprot/R1AB_WBV24 R1AB_WBV24] The 3C-like serine proteinase is responsible for the majority of cleavages. The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. | + | [https://www.uniprot.org/uniprot/R1AB_WBV24 R1AB_WBV24] Catalyzes the RNA N7-guanylyltransferase reaction to methylate the core cap structure GpppN-RNA into the type-0 cap (m)GpppN-RNA.<ref>PMID:36265859</ref> The 3C-like serine proteinase is responsible for the majority of cleavages.<ref>PMID:21068254</ref> The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. The exoribonuclease acts on ssRNA in a 3' to 5' direction (PubMed:30058998). Most active on dsRNA substrates containing one or two non-paired 3'-terminal nucleotides, thereby probably increasing the fidelity of the viral RNA-dependent RNA polymerase by excising RNA 3'-end mismatches during viral RNA replication (PubMed:30058998).<ref>PMID:30058998</ref> NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. Catalyzes the RNA 2'-O-ribose methyltransferase reaction to methylate the type-0 cap into the type-1 cap (m)GpppN(m)-RNA.[UniProtKB:P0C6X7] |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The order Nidovirales is a diverse group of (+)RNA viruses, with a common genome organization and conserved set of replicative and editing enzymes. In particular, RNA methyltransferases play a central role in mRNA stability and immune escape. However, their presence and distribution in different Nidovirales families is not homogeneous. In Coronaviridae, the best characterized family, two distinct methytransferases perform methylation of the N7-guanine and 2'-OH of the RNA-cap to generate a cap-1 structure (m7GpppNm). The genes of both of these enzymes are located in the ORF1b genomic region. While 2'-O-MTases can be identified for most other families based on conservation of both sequence motifs and genetic loci, identification of the N7-guanine methyltransferase has proved more challenging. Recently, we identified a putative N7-MTase domain in the ORF1a region (N7-MT-1a) of certain members of the large genome Tobaniviridae family. Here, we demonstrate that this domain indeed harbors N7-specific methyltransferase activity. We present its structure as the first N7-specific Rossmann-fold (RF) MTase identified for (+)RNA viruses, making it remarkably different from that of the known Coronaviridae ORF1b N7-MTase gene. We discuss the evolutionary implications of such an appearance in this unexpected location in the genome, which introduces a split-off in the classification of Tobaniviridae.
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| - | A second type of N7-guanine RNA cap methyltransferase in an unusual locus of a large RNA virus genome.,Shannon A, Sama B, Gauffre P, Guez T, Debart F, Vasseur JJ, Decroly E, Canard B, Ferron F Nucleic Acids Res. 2022 Oct 21. pii: 6761739. doi: 10.1093/nar/gkac876. PMID:36265859<ref>PMID:36265859</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 7z2j" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
R1AB_WBV24 Catalyzes the RNA N7-guanylyltransferase reaction to methylate the core cap structure GpppN-RNA into the type-0 cap (m)GpppN-RNA.[1] The 3C-like serine proteinase is responsible for the majority of cleavages.[2] The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. The exoribonuclease acts on ssRNA in a 3' to 5' direction (PubMed:30058998). Most active on dsRNA substrates containing one or two non-paired 3'-terminal nucleotides, thereby probably increasing the fidelity of the viral RNA-dependent RNA polymerase by excising RNA 3'-end mismatches during viral RNA replication (PubMed:30058998).[3] NendoU is a Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. Catalyzes the RNA 2'-O-ribose methyltransferase reaction to methylate the type-0 cap into the type-1 cap (m)GpppN(m)-RNA.[UniProtKB:P0C6X7]
References
- ↑ Shannon A, Sama B, Gauffre P, Guez T, Debart F, Vasseur JJ, Decroly E, Canard B, Ferron F. A second type of N7-guanine RNA cap methyltransferase in an unusual locus of a large RNA virus genome. Nucleic Acids Res. 2022 Oct 21. pii: 6761739. doi: 10.1093/nar/gkac876. PMID:36265859 doi:http://dx.doi.org/10.1093/nar/gkac876
- ↑ Ulferts R, Mettenleiter TC, Ziebuhr J. Characterization of Bafinivirus main protease autoprocessing activities. J Virol. 2011 Feb;85(3):1348-59. PMID:21068254 doi:10.1128/JVI.01716-10
- ↑ Durzynska I, Sauerwald M, Karl N, Madhugiri R, Ziebuhr J. Characterization of a bafinivirus exoribonuclease activity. J Gen Virol. 2018 Sep;99(9):1253-1260. PMID:30058998 doi:10.1099/jgv.0.001120
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