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10.1371/journal.ppat.1002294 http://scihub22266oqcxt.onion/10.1371/journal.ppat.1002294 22022266!3192843!22022266     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+Pathog 2011 ; 7 (10): e1002294 Nephropedia Template TP {{tp|p=22022266|t=2011. Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2 -O-methylation by nsp16/nsp10 protein complex |pdf=|usr=}}{{22022266}} gab.com Text Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2 -O-methylation by nsp16/nsp10 protein complex JO: PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=22022266 #FOAvip The 5'-cap structure is a distinct feature of eukaryotic mRNAs, and eukaryotic viruses generally modify the 5'-end of viral RNAs to mimic cellular mRNA structure, which is important for RNA stability, protein translation and viral immune escape. SARS coronavirus (SARS-CoV) encodes two S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTase) which sequentially methylate the RNA cap at guanosine-N7 and ribose 2'-O positions, catalyzed by nsp14 N7-MTase and nsp16 2'-O-MTase, respectively. A unique feature for SARS-CoV is that nsp16 requires non-structural protein nsp10 as a stimulatory factor to execute its MTase activity. Here we report the biochemical characterization of SARS-CoV 2'-O-MTase and the crystal structure of nsp16/nsp10 complex bound with methyl donor SAM. We found that SARS-CoV nsp16 MTase methylated m7GpppA-RNA but not m7GpppG-RNA, which is in contrast with nsp14 MTase that functions in a sequence-independent manner. We demonstrated that nsp10 is required for nsp16 to bind both m7GpppA-RNA substrate and SAM cofactor. Structural analysis revealed that nsp16 possesses the canonical scaffold of MTase and associates with nsp10 at 1ratio1 ratio. The structure of the nsp16/nsp10 interaction interface shows that nsp10 may stabilize the SAM-binding pocket and extend the substrate RNA-binding groove of nsp16, consistent with the findings in biochemical assays. These results suggest that nsp16/nsp10 interface may represent a better drug target than the viral MTase active site for developing highly specific anti-coronavirus drugs. Twit Text FOAVip Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2 -O-methylation by nsp16/nsp10 protein complex ????PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=22022266 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=22022266 #FOAvip English Wikipedia <ref>{{Cite pmid|22022266}}</ref> Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2 -O-methylation by nsp16/nsp10 protein complex #MMPMID22022266 Chen Y; Su C; Ke M; Jin X; Xu L; Zhang Z; Wu A; Sun Y; Yang Z; Tien P; Ahola T; Liang Y; Liu X; Guo D PLoS Pathog 2011[Oct]; 7 (10): e1002294 PMID22022266show ga The 5'-cap structure is a distinct feature of eukaryotic mRNAs, and eukaryotic viruses generally modify the 5'-end of viral RNAs to mimic cellular mRNA structure, which is important for RNA stability, protein translation and viral immune escape. SARS coronavirus (SARS-CoV) encodes two S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTase) which sequentially methylate the RNA cap at guanosine-N7 and ribose 2'-O positions, catalyzed by nsp14 N7-MTase and nsp16 2'-O-MTase, respectively. A unique feature for SARS-CoV is that nsp16 requires non-structural protein nsp10 as a stimulatory factor to execute its MTase activity. Here we report the biochemical characterization of SARS-CoV 2'-O-MTase and the crystal structure of nsp16/nsp10 complex bound with methyl donor SAM. We found that SARS-CoV nsp16 MTase methylated m7GpppA-RNA but not m7GpppG-RNA, which is in contrast with nsp14 MTase that functions in a sequence-independent manner. We demonstrated that nsp10 is required for nsp16 to bind both m7GpppA-RNA substrate and SAM cofactor. Structural analysis revealed that nsp16 possesses the canonical scaffold of MTase and associates with nsp10 at 1ratio1 ratio. The structure of the nsp16/nsp10 interaction interface shows that nsp10 may stabilize the SAM-binding pocket and extend the substrate RNA-binding groove of nsp16, consistent with the findings in biochemical assays. These results suggest that nsp16/nsp10 interface may represent a better drug target than the viral MTase active site for developing highly specific anti-coronavirus drugs. |Crystallography, X-Ray[MESH] |Methylation[MESH] |Methyltransferases/*chemistry/genetics/metabolism[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Protein Binding[MESH] |Protein Structure, Secondary[MESH] |Protein Structure, Tertiary[MESH] |RNA Cap Analogs/metabolism[MESH] |RNA Caps/chemistry/metabolism[MESH] |RNA, Viral/genetics/*metabolism[MESH] |S-Adenosylmethionine/metabolism[MESH] |Severe acute respiratory syndrome-related coronavirus/genetics/*metabolism[MESH]Biochemical and structural insights into the mechanisms of SARS corona(epmc).pdf DeepDyve Pubget Overpricing