Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family.
Identifieur interne : 002147 ( PubMed/Corpus ); précédent : 002146; suivant : 002148Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family.
Auteurs : Stefano Ricagno ; Marie-Pierre Egloff ; Rachel Ulferts ; Bruno Coutard ; Didier Nurizzo ; Valérie Campanacci ; Christian Cambillau ; John Ziebuhr ; Bruno CanardSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.
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 approximately 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(2+)-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-A 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.
DOI: 10.1073/pnas.0601708103
PubMed: 16882730
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pubmed:16882730Le document en format XML
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sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name></author><author><name sortKey="Nurizzo, Didier" sort="Nurizzo, Didier" uniqKey="Nurizzo D" first="Didier" last="Nurizzo">Didier Nurizzo</name></author><author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16882730</idno><idno 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first="Marie-Pierre" last="Egloff">Marie-Pierre Egloff</name></author><author><name sortKey="Ulferts, Rachel" sort="Ulferts, Rachel" uniqKey="Ulferts R" first="Rachel" last="Ulferts">Rachel Ulferts</name></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name></author><author><name sortKey="Nurizzo, Didier" sort="Nurizzo, Didier" uniqKey="Nurizzo D" first="Didier" last="Nurizzo">Didier Nurizzo</name></author><author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><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><term>Viral Nonstructural Proteins (chemistry)</term><term>Virus Replication</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Endoribonucleases</term><term>RNA Replicase</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endonucleases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term><term>Virus Replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The approximately 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(2+)-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-A 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16882730</PMID><DateCompleted><Year>2006</Year><Month>09</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>103</Volume><Issue>32</Issue><PubDate><Year>2006</Year><Month>Aug</Month><Day>08</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family.</ArticleTitle><Pagination><MedlinePgn>11892-7</MedlinePgn></Pagination><Abstract><AbstractText>The approximately 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(2+)-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-A 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ricagno</LastName><ForeName>Stefano</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Case 925, Ecole d'Ingénieurs de Luminy, Architecture et Fonction des Macromolécules Biologiques, Unité Mixte de Recherche 6098, Centre National de la Recherche Scientifique and Universités d'Aix-Marseille I et II, 13288 Marseille Cedex 9, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Egloff</LastName><ForeName>Marie-Pierre</ForeName><Initials>MP</Initials></Author><Author ValidYN="Y"><LastName>Ulferts</LastName><ForeName>Rachel</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Nurizzo</LastName><ForeName>Didier</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Campanacci</LastName><ForeName>Valérie</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Cambillau</LastName><ForeName>Christian</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Ziebuhr</LastName><ForeName>John</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2H85</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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