SrasV1, France, Analysis, bibRecord, 000308

Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family

Identifieur interne : 000308 ( France/Analysis ); précédent : 000307; suivant : 000309

Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family

Auteurs : Stefano Ricagno ; Marie-Pierre Egloff ; Rachel Ulferts [Royaume-Uni] ; Bruno Coutard ; Didier Nurizzo [France] ; Valérie Campanacci [France] ; Christian Cambillau [France] ; John Ziebuhr [Royaume-Uni] ; Bruno Canard

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.

RBID : PMC:2131687

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Endonucleases (metabolism), Endoribonucleases (chemistry), Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Tertiary, RNA Replicase (chemistry), SARS Virus (metabolism), Sequence Homology, Amino Acid, Viral Nonstructural Proteins (chemistry), Virus Replication.
MESH :
- chemical , chemistry : Endoribonucleases, RNA Replicase, Viral Nonstructural Proteins.
- chemical , metabolism : Endonucleases.
- metabolism : SARS Virus.
- Amino Acid Sequence, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Virus Replication.

Abstract

The ≈30-kb coronavirus (+)RNA genome is replicated and transcribed by a membrane-bound replicase complex made up of 16 viral nonstructural proteins (nsp) with multiple enzymatic activities. The complex includes an RNA endonuclease, NendoU, that is conserved among nidoviruses but no other RNA virus, making it a genetic marker of this virus order. NendoU (nsp15) is a Mn²⁺-dependent, uridylate-specific enzyme, which leaves 2′–3′-cyclic phosphates 5′ to the cleaved bond. Neither biochemical nor sequence homology criteria allow a classification of nsp15 into existing endonuclease families. Here, we report the crystal structure of the severe acute respiratory syndrome coronavirus nsp15 at 2.6-Å resolution. Nsp15 exhibits a unique fold and assembles into a toric hexamer with six potentially active, peripheric catalytic sites. The structure and the spatial arrangement of the catalytic residues into an RNase A-like active site define a separate endonuclease family, endoU, and represent another spectacular example of convergent evolution toward an enzymatic function that is critically involved in the coronavirus replication cycle.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2131687

DOI: 10.1073/pnas.0601708103
PubMed: 16882730
PubMed Central: 2131687

Affiliations:

Links to Exploration step

PMC:2131687

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Binding Sites</term>
<term>Catalytic Domain</term>
<term>Crystallography, X-Ray</term>
<term>Endonucleases (metabolism)</term>
<term>Endoribonucleases (chemistry)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Conformation</term>
<term>Protein Structure, Tertiary</term>
<term>RNA Replicase (chemistry)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Virus Replication</term>
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<term>Cristallographie aux rayons X</term>
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<term>Données de séquences moléculaires</term>
<term>Endonucleases (métabolisme)</term>
<term>Endoribonucleases ()</term>
<term>Modèles moléculaires</term>
<term>Protéines virales non structurales ()</term>
<term>RNA replicase ()</term>
<term>Réplication virale</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Sites de fixation</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS (métabolisme)</term>
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<term>Viral Nonstructural Proteins</term>
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<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Données de séquences moléculaires</term>
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<term>Modèles moléculaires</term>
<term>Protéines virales non structurales</term>
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<term>Similitude de séquences d'acides aminés</term>
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<front><div type="abstract" xml:lang="en"><p>The ≈30-kb coronavirus (+)RNA genome is replicated and transcribed by a membrane-bound replicase complex made up of 16 viral nonstructural proteins (nsp) with multiple enzymatic activities. The complex includes an RNA endonuclease, NendoU, that is conserved among nidoviruses but no other RNA virus, making it a genetic marker of this virus order. NendoU (nsp15) is a Mn<sup>2+</sup>
-dependent, uridylate-specific enzyme, which leaves 2′–3′-cyclic phosphates 5′ to the cleaved bond. Neither biochemical nor sequence homology criteria allow a classification of nsp15 into existing endonuclease families. Here, we report the crystal structure of the severe acute respiratory syndrome coronavirus nsp15 at 2.6-Å resolution. Nsp15 exhibits a unique fold and assembles into a toric hexamer with six potentially active, peripheric catalytic sites. The structure and the spatial arrangement of the catalytic residues into an RNase A-like active site define a separate endonuclease family, endoU, and represent another spectacular example of convergent evolution toward an enzymatic function that is critically involved in the coronavirus replication cycle.</p>
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Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family

Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family

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