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" The crystal structure of nsp10-nsp16 heterodimer from SARS-CoV-2 in complex with S-adenosylmethionine. "
Rosas-Lemus, Monica; Minasov, George; Shuvalova, Ludmilla; Inniss, Nicole L; Kiryukhina, Olga; Wiersum, Grant; Kim, Youngchang; Jedrzejczak, Robert; Maltseva, Natalia I; Endres, Michael; Jaroszewski, Lukasz; Godzik, Adam; Joachimiak, Andrzej; Satchell, Karla JF
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AL
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912780
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LA1n13w9fx
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| Title & Author
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The crystal structure of nsp10-nsp16 heterodimer from SARS-CoV-2 in complex with S-adenosylmethionine. [Article]\ Rosas-Lemus, Monica; Minasov, George; Shuvalova, Ludmilla; Inniss, Nicole L; Kiryukhina, Olga; Wiersum, Grant; Kim, Youngchang; Jedrzejczak, Robert; Maltseva, Natalia I; Endres, Michael; Jaroszewski, Lukasz; Godzik, Adam; Joachimiak, Andrzej; Satchell, Karla JF
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2020
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UC Riverside
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SARS-CoV-2 is a member of the coronaviridae family and is the etiological agent of the respiratory Coronavirus Disease 2019. The virus has spread rapidly around the world resulting in over two million cases and nearly 150,000 deaths as of April 17, 2020. Since no treatments or vaccines are available to treat COVID-19 and SARS-CoV-2, respiratory complications derived from the infections have overwhelmed healthcare systems around the world. This virus is related to SARS-CoV-1, the virus that caused the 2002-2004 outbreak of Severe Acute Respiratory Syndrome. In January 2020, the Center for Structural Genomics of Infectious Diseases implemented a structural genomics pipeline to solve the structures of proteins essential for coronavirus replication-transcription. Here we show the first structure of the SARS-CoV-2 nsp10-nsp16 2'-O-methyltransferase complex with S-adenosylmethionine at a resolution of 1.80 Å. This heterodimer complex is essential for capping viral mRNA transcripts for efficient translation and to evade immune surveillance.
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