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Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex
To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1–16), amongst which two methyltran...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053173/ https://www.ncbi.nlm.nih.gov/pubmed/21393853 http://dx.doi.org/10.1107/S1744309111002867 |
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author | Debarnot, Claire Imbert, Isabelle Ferron, François Gluais, Laure Varlet, Isabelle Papageorgiou, Nicolas Bouvet, Mickaël Lescar, Julien Decroly, Etienne Canard, Bruno |
author_facet | Debarnot, Claire Imbert, Isabelle Ferron, François Gluais, Laure Varlet, Isabelle Papageorgiou, Nicolas Bouvet, Mickaël Lescar, Julien Decroly, Etienne Canard, Bruno |
author_sort | Debarnot, Claire |
collection | PubMed |
description | To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1–16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. The crystal structure of nsp16 is unknown. Nsp16 is an RNA-cap AdoMet-dependent (nucleoside-2′-O-)-methyltransferase that is only active in the presence of nsp10. In this paper, the expression, purification and crystallization of nsp10 in complex with nsp16 are reported. The crystals diffracted to a resolution of 1.9 Å resolution and crystal structure determination is in progress. |
format | Text |
id | pubmed-3053173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-30531732013-03-01 Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex Debarnot, Claire Imbert, Isabelle Ferron, François Gluais, Laure Varlet, Isabelle Papageorgiou, Nicolas Bouvet, Mickaël Lescar, Julien Decroly, Etienne Canard, Bruno Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications To date, the SARS coronavirus is the only known highly pathogenic human coronavirus. In 2003, it was responsible for a large outbreak associated with a 10% fatality rate. This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1–16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. The crystal structure of nsp16 is unknown. Nsp16 is an RNA-cap AdoMet-dependent (nucleoside-2′-O-)-methyltransferase that is only active in the presence of nsp10. In this paper, the expression, purification and crystallization of nsp10 in complex with nsp16 are reported. The crystals diffracted to a resolution of 1.9 Å resolution and crystal structure determination is in progress. International Union of Crystallography 2011-02-25 /pmc/articles/PMC3053173/ /pubmed/21393853 http://dx.doi.org/10.1107/S1744309111002867 Text en © International Union of Crystallography 2011 |
spellingShingle | Crystallization Communications Debarnot, Claire Imbert, Isabelle Ferron, François Gluais, Laure Varlet, Isabelle Papageorgiou, Nicolas Bouvet, Mickaël Lescar, Julien Decroly, Etienne Canard, Bruno Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title | Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title_full | Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title_fullStr | Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title_full_unstemmed | Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title_short | Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex |
title_sort | crystallization and diffraction analysis of the sars coronavirus nsp10–nsp16 complex |
topic | Crystallization Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053173/ https://www.ncbi.nlm.nih.gov/pubmed/21393853 http://dx.doi.org/10.1107/S1744309111002867 |
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