Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.
Identifieur interne : 002306 ( Ncbi/Checkpoint ); précédent : 002305; suivant : 002307Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.
Auteurs : Claire Debarnot [France] ; Isabelle Imbert ; François Ferron ; Laure Gluais ; Isabelle Varlet ; Nicolas Papageorgiou ; Mickaël Bouvet ; Julien Lescar ; Etienne Decroly ; Bruno CanardSource :
- Acta crystallographica. Section F, Structural biology and crystallization communications [ 1744-3091 ] ; 2011.
Descripteurs français
- KwdFr :
- Clonage moléculaire, Cristallisation, Cristallographie aux rayons X, Données de séquences moléculaires, Humains, Methyltransferases (), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (isolement et purification), RNA replicase (), RNA replicase (génétique), RNA replicase (isolement et purification), Virus du SRAS ().
- MESH :
- génétique : Protéines virales non structurales, RNA replicase.
- isolement et purification : Protéines virales non structurales, RNA replicase.
- Clonage moléculaire, Cristallisation, Cristallographie aux rayons X, Données de séquences moléculaires, Humains, Methyltransferases, Protéines virales non structurales, RNA replicase, Virus du SRAS.
English descriptors
- KwdEn :
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Humans, Methyltransferases (chemistry), Molecular Sequence Data, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (isolation & purification), SARS Virus (chemistry), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification).
- MESH :
- chemical , chemistry : Methyltransferases, RNA Replicase, Viral Nonstructural Proteins.
- chemical , genetics : RNA Replicase, Viral Nonstructural Proteins.
- chemical , isolation & purification : RNA Replicase, Viral Nonstructural Proteins.
- chemistry : SARS Virus.
- Cloning, Molecular, Crystallization, Crystallography, X-Ray, Humans, Molecular Sequence Data.
Abstract
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.
DOI: 10.1107/S1744309111002867
PubMed: 21393853
Affiliations:
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pubmed:21393853Le document en format XML
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<term>Molecular Sequence Data</term>
<term>RNA Replicase (chemistry)</term>
<term>RNA Replicase (genetics)</term>
<term>RNA Replicase (isolation & purification)</term>
<term>SARS Virus (chemistry)</term>
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<term>Viral Nonstructural Proteins (genetics)</term>
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<term>RNA replicase (isolement et purification)</term>
<term>Virus du SRAS ()</term>
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<term>RNA Replicase</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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