Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Debarnot, Claire, Imbert, Isabelle, Ferron, François, Gluais, Laure, Varlet, Isabelle, Papageorgiou, Nicolas, Bouvet, Mickaël, Lescar, Julien, Decroly, Etienne, Canard, Bruno
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2011
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
_version_ 1782199708951773184
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
work_keys_str_mv AT debarnotclaire crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT imbertisabelle crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT ferronfrancois crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT gluaislaure crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT varletisabelle crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT papageorgiounicolas crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT bouvetmickael crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT lescarjulien crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT decrolyetienne crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex
AT canardbruno crystallizationanddiffractionanalysisofthesarscoronavirusnsp10nsp16complex