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Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (21): ä Nephropedia Template TP
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2 -O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography #MMPMID33972410
Wilamowski M; Sherrell DA; Minasov G; Kim Y; Shuvalova L; Lavens A; Chard R; Maltseva N; Jedrzejczak R; Rosas-Lemus M; Saint N; Foster IT; Michalska K; Satchell KJF; Joachimiak A
Proc Natl Acad Sci U S A 2021[May]; 118 (21): ä PMID33972410show ga
The genome of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) coronavirus has a capping modification at the 5'-untranslated region (UTR) to prevent its degradation by host nucleases. These modifications are performed by the Nsp10/14 and Nsp10/16 heterodimers using S-adenosylmethionine as the methyl donor. Nsp10/16 heterodimer is responsible for the methylation at the ribose 2'-O position of the first nucleotide. To investigate the conformational changes of the complex during 2'-O methyltransferase activity, we used a fixed-target serial synchrotron crystallography method at room temperature. We determined crystal structures of Nsp10/16 with substrates and products that revealed the states before and after methylation, occurring within the crystals during the experiments. Here we report the crystal structure of Nsp10/16 in complex with Cap-1 analog ((m7)GpppA(m2'-O)). Inhibition of Nsp16 activity may reduce viral proliferation, making this protein an attractive drug target.