Structural Biology of the Arterivirus nsp11 Endoribonucleases.
Identifieur interne : 000B78 ( Main/Exploration ); précédent : 000B77; suivant : 000B79Structural Biology of the Arterivirus nsp11 Endoribonucleases.
Auteurs : Manfeng Zhang [République populaire de Chine] ; Xiaorong Li [République populaire de Chine] ; Zengqin Deng [République populaire de Chine] ; Zhenhang Chen [République populaire de Chine] ; Yang Liu [République populaire de Chine] ; Yina Gao [République populaire de Chine] ; Wei Wu [République populaire de Chine] ; Zhongzhou Chen [République populaire de Chine]Source :
- Journal of virology [ 1098-5514 ] ; 2017.
Descripteurs français
- KwdFr :
- Alignement de séquences, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (génétique), Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme), Cristallographie aux rayons X, Domaine catalytique, Domaines protéiques, Endoribonucleases (), Endoribonucleases (génétique), Endoribonucleases (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Structure secondaire des protéines, Séquence conservée, Séquence d'acides aminés, Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (métabolisme), Virus du syndrome respiratoire et reproducteur porcin (), Virus du syndrome respiratoire et reproducteur porcin (enzymologie).
- MESH :
- enzymologie : Virus du syndrome respiratoire et reproducteur porcin.
- génétique : Coronavirus du syndrome respiratoire du Moyen-Orient, Endoribonucleases, Escherichia coli, Protéines recombinantes, Protéines virales non structurales, Virus du SRAS.
- métabolisme : Coronavirus du syndrome respiratoire du Moyen-Orient, Endoribonucleases, Escherichia coli, Protéines recombinantes, Protéines virales non structurales, Virus du SRAS.
- Alignement de séquences, Coronavirus du syndrome respiratoire du Moyen-Orient, Cristallographie aux rayons X, Domaine catalytique, Domaines protéiques, Endoribonucleases, Expression des gènes, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines recombinantes, Protéines virales non structurales, Structure secondaire des protéines, Séquence conservée, Séquence d'acides aminés, Virus du SRAS, Virus du syndrome respiratoire et reproducteur porcin.
English descriptors
- KwdEn :
- Amino Acid Sequence, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Endoribonucleases (chemistry), Endoribonucleases (genetics), Endoribonucleases (metabolism), Equartevirus (chemistry), Equartevirus (enzymology), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression, Middle East Respiratory Syndrome Coronavirus (chemistry), Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (metabolism), Models, Molecular, Mutation, Porcine respiratory and reproductive syndrome virus (chemistry), Porcine respiratory and reproductive syndrome virus (enzymology), Protein Domains, Protein Multimerization, Protein Structure, Secondary, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (chemistry), SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , genetics : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : Endoribonucleases, Recombinant Proteins, Viral Nonstructural Proteins.
- chemistry : Equartevirus, Middle East Respiratory Syndrome Coronavirus, Porcine respiratory and reproductive syndrome virus, SARS Virus.
- enzymology : Equartevirus, Porcine respiratory and reproductive syndrome virus.
- genetics : Escherichia coli, Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- metabolism : Escherichia coli, Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- Amino Acid Sequence, Catalytic Domain, Conserved Sequence, Crystallography, X-Ray, Gene Expression, Models, Molecular, Mutation, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Sequence Alignment.
Abstract
Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.
DOI: 10.1128/JVI.01309-16
PubMed: 27795409
Affiliations:
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Le document en format XML
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<term>Catalytic Domain</term>
<term>Conserved Sequence</term>
<term>Crystallography, X-Ray</term>
<term>Endoribonucleases (chemistry)</term>
<term>Endoribonucleases (genetics)</term>
<term>Endoribonucleases (metabolism)</term>
<term>Equartevirus (chemistry)</term>
<term>Equartevirus (enzymology)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Gene Expression</term>
<term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term>
<term>Middle East Respiratory Syndrome Coronavirus (genetics)</term>
<term>Middle East Respiratory Syndrome Coronavirus (metabolism)</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Porcine respiratory and reproductive syndrome virus (chemistry)</term>
<term>Porcine respiratory and reproductive syndrome virus (enzymology)</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Alignment</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term>
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<term>Coronavirus du syndrome respiratoire du Moyen-Orient (métabolisme)</term>
<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Domaines protéiques</term>
<term>Endoribonucleases ()</term>
<term>Endoribonucleases (génétique)</term>
<term>Endoribonucleases (métabolisme)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Expression des gènes</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Mutation</term>
<term>Protéines recombinantes ()</term>
<term>Protéines recombinantes (génétique)</term>
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<term>Virus du SRAS (métabolisme)</term>
<term>Virus du syndrome respiratoire et reproducteur porcin ()</term>
<term>Virus du syndrome respiratoire et reproducteur porcin (enzymologie)</term>
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<term>Middle East Respiratory Syndrome Coronavirus</term>
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<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Virus du SRAS</term>
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<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Virus du SRAS</term>
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<term>Conserved Sequence</term>
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<term>Gene Expression</term>
<term>Models, Molecular</term>
<term>Mutation</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Secondary</term>
<term>Sequence Alignment</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
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<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Domaines protéiques</term>
<term>Endoribonucleases</term>
<term>Expression des gènes</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Mutation</term>
<term>Protéines recombinantes</term>
<term>Protéines virales non structurales</term>
<term>Structure secondaire des protéines</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Endoribonuclease (NendoU) is unique and conserved as a major genetic marker in nidoviruses that infect vertebrate hosts. Arterivirus nonstructural protein 11 (nsp11) was shown to have NendoU activity and play essential roles in the viral life cycle. Here, we report three crystal structures of porcine reproductive and respiratory syndrome virus (PRRSV) and equine arteritis virus (EAV) nsp11 mutants. The structures of arterivirus nsp11 contain two conserved compact domains: the N-terminal domain (NTD) and C-terminal domain (CTD). The structures of PRRSV and EAV endoribonucleases are similar and conserved in the arterivirus, but they are greatly different from that of severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS) coronaviruses (CoV), representing important human pathogens in the Nidovirales order. The catalytic center of NendoU activity is located in the CTD, where a positively charged groove is next to the key catalytic residues conserved in nidoviruses. Although the NTD is nearly identical, the catalytic region of the arterivirus nsp11 family proteins is remarkably flexible, and the oligomerization may be concentration dependent. In summary, our structures provide new insight into this key multifunctional NendoU family of proteins and lay a foundation for better understanding of the molecular mechanism and antiviral drug development.</div>
</front>
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<name sortKey="Li, Xiaorong" sort="Li, Xiaorong" uniqKey="Li X" first="Xiaorong" last="Li">Xiaorong Li</name>
<name sortKey="Liu, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang Liu</name>
<name sortKey="Wu, Wei" sort="Wu, Wei" uniqKey="Wu W" first="Wei" last="Wu">Wei Wu</name>
</country>
</tree>
</affiliations>
</record>
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