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10.1126/scisignal.abh2071 http://scihub22266oqcxt.onion/10.1126/scisignal.abh2071 34131072!8432954!34131072     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Signal 2021 ; 14 (689): ä Nephropedia Template TP {{tp|p=34131072|t=2021. Mn(2+) coordinates Cap-0-RNA to align substrates for efficient 2 -O-methyl transfer by SARS-CoV-2 nsp16 |pdf=|usr=}}{{34131072}} gab.com Text Mn(2+) coordinates Cap-0-RNA to align substrates for efficient 2 -O-methyl transfer by SARS-CoV-2 nsp16 JO: Sci Signal http://www.kidney.de/pget.php?&tw=1&pmid=34131072 #FOAvip Capping of viral messenger RNAs is essential for efficient translation, for virus replication, and for preventing detection by the host cell innate response system. The SARS-CoV-2 genome encodes the 2'-O-methyltransferase nsp16, which, when bound to the coactivator nsp10, uses S-adenosylmethionine (SAM) as a donor to transfer a methyl group to the first ribonucleotide of the mRNA in the final step of viral mRNA capping. Here, we provide biochemical and structural evidence that this reaction requires divalent cations, preferably Mn(2+), and a coronavirus-specific four-residue insert. We determined the x-ray structures of the SARS-CoV-2 2'-O-methyltransferase (the nsp16-nsp10 heterodimer) in complex with its reaction substrates, products, and divalent metal cations. These structural snapshots revealed that metal ions and the insert stabilize interactions between the capped RNA and nsp16, resulting in the precise alignment of the ribonucleotides in the active site. Comparison of available structures of 2'-O-methyltransferases with capped RNAs from different organisms revealed that the four-residue insert unique to coronavirus nsp16 alters the backbone conformation of the capped RNA in the binding groove, thereby promoting catalysis. This insert is highly conserved across coronaviruses, and its absence in mammalian methyltransferases makes this region a promising site for structure-guided drug design of selective coronavirus inhibitors. Twit Text FOAVip Mn(2+) coordinates Cap-0-RNA to align substrates for efficient 2 -O-methyl transfer by SARS-CoV-2 nsp16 ????Sci Signal http://www.kidney.de/pget.php?&tw=1&pmid=34131072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34131072 #FOAvip English Wikipedia <ref>{{Cite pmid|34131072}}</ref> Mn(2+) coordinates Cap-0-RNA to align substrates for efficient 2 -O-methyl transfer by SARS-CoV-2 nsp16 #MMPMID34131072 Minasov G; Rosas-Lemus M; Shuvalova L; Inniss NL; Brunzelle JS; Daczkowski CM; Hoover P; Mesecar AD; Satchell KJF Sci Signal 2021[Jun]; 14 (689): ä PMID34131072show ga Capping of viral messenger RNAs is essential for efficient translation, for virus replication, and for preventing detection by the host cell innate response system. The SARS-CoV-2 genome encodes the 2'-O-methyltransferase nsp16, which, when bound to the coactivator nsp10, uses S-adenosylmethionine (SAM) as a donor to transfer a methyl group to the first ribonucleotide of the mRNA in the final step of viral mRNA capping. Here, we provide biochemical and structural evidence that this reaction requires divalent cations, preferably Mn(2+), and a coronavirus-specific four-residue insert. We determined the x-ray structures of the SARS-CoV-2 2'-O-methyltransferase (the nsp16-nsp10 heterodimer) in complex with its reaction substrates, products, and divalent metal cations. These structural snapshots revealed that metal ions and the insert stabilize interactions between the capped RNA and nsp16, resulting in the precise alignment of the ribonucleotides in the active site. Comparison of available structures of 2'-O-methyltransferases with capped RNAs from different organisms revealed that the four-residue insert unique to coronavirus nsp16 alters the backbone conformation of the capped RNA in the binding groove, thereby promoting catalysis. This insert is highly conserved across coronaviruses, and its absence in mammalian methyltransferases makes this region a promising site for structure-guided drug design of selective coronavirus inhibitors. |Amino Acid Sequence[MESH] |COVID-19/*virology[MESH] |Catalytic Domain[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Manganese/metabolism[MESH] |Methylation[MESH] |Methyltransferases/chemistry/genetics/metabolism[MESH] |Models, Molecular[MESH] |Nucleic Acid Conformation[MESH] |RNA Caps/chemistry/genetics/*metabolism[MESH] |RNA Stability[MESH] |RNA, Messenger/chemistry/genetics/metabolism[MESH] |RNA, Viral/chemistry/genetics/*metabolism[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH] |S-Adenosylmethionine/chemistry/metabolism[MESH] |SARS-CoV-2/genetics/*metabolism[MESH] |Signal Transduction[MESH] |Substrate Specificity[MESH]Mn(2+) coordinates Cap-0-RNA to align substrates for efficient 2 -O-me(epmc).pdf DeepDyve Pubget Overpricing