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10.1038/s41467-021-23594-y http://scihub22266oqcxt.onion/10.1038/s41467-021-23594-y 34078893!8172916!34078893     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34078893&cmd=llinks): Failed to open stream: HTTP request failed! 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A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2 -O methylation of its first nucleotide |pdf=|usr=}}{{34078893}} gab.com Text A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2 -O methylation of its first nucleotide JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34078893 #FOAvip The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'-O methylation of the first nucleotide converts the status of mRNA cap from Cap-0 to Cap-1, and thus, helps the virus evade immune surveillance in host cells. Here, we report two structures of nsp16/nsp10 representing pre- and post-release states of the RNA product (Cap-1). We observe overall widening of the enzyme upon product formation, and an inward twisting motion in the substrate binding region upon product release. These conformational changes reset the enzyme for the next round of catalysis. The structures also identify a unique binding mode and the importance of a divalent metal ion for 2'-O methylation. We also describe underlying structural basis for the perturbed enzymatic activity of a clinical variant of SARS-CoV-2, and a previous SARS-CoV outbreak strain. Twit Text FOAVip A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2 -O methylation of its first nucleotide ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=34078893 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34078893 #FOAvip English Wikipedia <ref>{{Cite pmid|34078893}}</ref> A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2 -O methylation of its first nucleotide #MMPMID34078893 Viswanathan T; Misra A; Chan SH; Qi S; Dai N; Arya S; Martinez-Sobrido L; Gupta YK Nat Commun 2021[Jun]; 12 (1): 3287 PMID34078893show ga The SARS-CoV-2 nsp16/nsp10 enzyme complex modifies the 2'-OH of the first transcribed nucleotide of the viral mRNA by covalently attaching a methyl group to it. The 2'-O methylation of the first nucleotide converts the status of mRNA cap from Cap-0 to Cap-1, and thus, helps the virus evade immune surveillance in host cells. Here, we report two structures of nsp16/nsp10 representing pre- and post-release states of the RNA product (Cap-1). We observe overall widening of the enzyme upon product formation, and an inward twisting motion in the substrate binding region upon product release. These conformational changes reset the enzyme for the next round of catalysis. The structures also identify a unique binding mode and the importance of a divalent metal ion for 2'-O methylation. We also describe underlying structural basis for the perturbed enzymatic activity of a clinical variant of SARS-CoV-2, and a previous SARS-CoV outbreak strain. |Amino Acid Sequence[MESH] |Binding Sites[MESH] |Biocatalysis[MESH] |Cloning, Molecular[MESH] |Crystallography, X-Ray[MESH] |Escherichia coli/genetics/metabolism[MESH] |Gene Expression Regulation, Viral[MESH] |Humans[MESH] |Magnesium/*chemistry/metabolism[MESH] |Methylation[MESH] |Methyltransferases[MESH] |Models, Molecular[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |RNA Caps/chemistry/genetics/*metabolism[MESH] |RNA, Viral/chemistry/genetics/*metabolism[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH] |S-Adenosylmethionine/chemistry/metabolism[MESH] |SARS-CoV-2/enzymology/*genetics/ultrastructure[MESH] |Sequence Alignment[MESH] |Sequence Homology, Amino Acid[MESH] |Substrate Specificity[MESH] |Viral Nonstructural Proteins/chemistry/genetics/*metabolism[MESH]A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2 -O methylatio(epmc).pdf DeepDyve Pubget Overpricing