Non-structural protein NSP8 superfamily, coronavirus
Short name | NSP8_sf_CoV |
Overlapping entries |
Description
References
1.Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic. Lubin JH, Zardecki C, Dolan EM, Lu C, Shen Z, Dutta S, Westbrook JD, Hudson BP, Goodsell DS, Williams JK, Voigt M, Sarma V, Xie L, Venkatachalam T, Arnold S, Alfaro Alvarado LH, Catalfano K, Khan A, McCarthy E, Staggers S, Tinsley B, Trudeau A, Singh J, Whitmore L, Zheng H, Benedek M, Currier J, Dresel M, Duvvuru A, Dyszel B, Fingar E, Hennen EM, Kirsch M, Khan AA, Labrie-Cleary C, Laporte S, Lenkeit E, Martin K, Orellana M, Ortiz-Alvarez de la Campa M, Paredes I, Wheeler B, Rupert A, Sam A, See K, Soto Zapata S, Craig PA, Hall BL, Jiang J, Koeppe JR, Mills SA, Pikaart MJ, Roberts R, Bromberg Y, Hoyer JS, Duffy S, Tischfield J, Ruiz FX, Arnold E, Baum J, Sandberg J, Brannigan G, Khare SD, Burley SK. Proteins (2021). PMID: 34580920
2.NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5. Johnson MA, Jaudzems K, Wuthrich K. J Mol Biol 402, 619-28, (2010). PMID: 20709084
3.A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus. Imbert I, Guillemot JC, Bourhis JM, Bussetta C, Coutard B, Egloff MP, Ferron F, Gorbalenya AE, Canard B. EMBO J 25, 4933-42, (2006). PMID: 17024178
4.Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer. Zhai Y, Sun F, Li X, Pang H, Xu X, Bartlam M, Rao Z. Nat. Struct. Mol. Biol. 12, 980-6, (2005). View articlePMID: 16228002
5.Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Kirchdoerfer RN, Ward AB. Nat Commun 10, 2342, (2019). PMID: 31138817
6.Identification and Characterization of a Human Coronavirus 229E Nonstructural Protein 8-Associated RNA 3'-Terminal Adenylyltransferase Activity. Tvarogova J, Madhugiri R, Bylapudi G, Ferguson LJ, Karl N, Ziebuhr J. J. Virol. 93, (2019). PMID: 30918070
7.The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension. te Velthuis AJ, van den Worm SH, Snijder EJ. Nucleic Acids Res. 40, 1737-47, (2012). PMID: 22039154
8.Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase. Wang Q, Wu J, Wang H, Gao Y, Liu Q, Mu A, Ji W, Yan L, Zhu Y, Zhu C, Fang X, Yang X, Huang Y, Gao H, Liu F, Ge J, Sun Q, Yang X, Xu W, Liu Z, Yang H, Lou Z, Jiang B, Guddat LW, Gong P, Rao Z. Cell 182, 417-428.e13, (2020). PMID: 32526208
9.SARS-CoV-2 Disrupts Splicing, Translation, and Protein Trafficking to Suppress Host Defenses. Banerjee AK, Blanco MR, Bruce EA, Honson DD, Chen LM, Chow A, Bhat P, Ollikainen N, Quinodoz SA, Loney C, Thai J, Miller ZD, Lin AE, Schmidt MM, Stewart DG, Goldfarb D, De Lorenzo G, Rihn SJ, Voorhees RM, Botten JW, Majumdar D, Guttman M. Cell 183, 1325-1339.e21, (2020). PMID: 33080218
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entries
- CATH-Gene3D:G3DSA:3.30.70.3540
- SUPERFAMILY:SSF143076