Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family
Identifieur interne : 001144 ( Pmc/Checkpoint ); précédent : 001143; suivant : 001145Crystal 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 CanardSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2006.
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:
DOI: 10.1073/pnas.0601708103
PubMed: 16882730
PubMed Central: 2131687
Affiliations:
- France, Royaume-Uni
- Auvergne-Rhône-Alpes, Provence-Alpes-Côte d'Azur, Rhône-Alpes
- Grenoble, Marseille
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and" id="aff3">Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom</nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL</wicri:regionArea><wicri:noRegion>Belfast BT9 7BL</wicri:noRegion></affiliation></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><affiliation><nlm:aff id="aff1">Cases *925 and</nlm:aff></affiliation></author><author><name sortKey="Nurizzo, Didier" sort="Nurizzo, Didier" uniqKey="Nurizzo D" first="Didier" last="Nurizzo">Didier Nurizzo</name><affiliation wicri:level="3"><nlm:aff id="aff4">European Synchrotron Radiation Facility, ID23, B.P. 220, F-38043 Grenoble Cedex, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>European Synchrotron Radiation Facility, ID23, B.P. 220, F-38043 Grenoble Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Grenoble</settlement></placeName></affiliation></author><author><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name><affiliation wicri:level="3"><nlm:aff id="aff2">932, 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, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France;</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>932, 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, 163 Avenue de Luminy, 13288 Marseille Cedex 9</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name><affiliation wicri:level="3"><nlm:aff id="aff2">932, 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, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France;</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>932, 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, 163 Avenue de Luminy, 13288 Marseille Cedex 9</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name><affiliation wicri:level="1"><nlm:aff wicri:cut="; and" id="aff3">Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom</nlm:aff><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL</wicri:regionArea><wicri:noRegion>Belfast BT9 7BL</wicri:noRegion></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation><nlm:aff id="aff1">Cases *925 and</nlm:aff></affiliation></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><idno type="eISSN">1091-6490</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16882730</article-id><article-id pub-id-type="pmc">2131687</article-id><article-id pub-id-type="publisher-id">3081</article-id><article-id pub-id-type="doi">10.1073/pnas.0601708103</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ricagno</surname><given-names>Stefano</given-names></name><xref ref-type="aff" rid="aff1">*</xref></contrib><contrib contrib-type="author"><name><surname>Egloff</surname><given-names>Marie-Pierre</given-names></name><xref ref-type="aff" rid="aff1">*</xref></contrib><contrib contrib-type="author"><name><surname>Ulferts</surname><given-names>Rachel</given-names></name><xref ref-type="aff" rid="aff3"><sup>†</sup></xref></contrib><contrib contrib-type="author"><name><surname>Coutard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="aff1">*</xref></contrib><contrib contrib-type="author"><name><surname>Nurizzo</surname><given-names>Didier</given-names></name><xref ref-type="aff" rid="aff4"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Campanacci</surname><given-names>Valérie</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Cambillau</surname><given-names>Christian</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ziebuhr</surname><given-names>John</given-names></name><xref ref-type="aff" rid="aff3"><sup>†</sup></xref></contrib><contrib contrib-type="author"><name><surname>Canard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="aff1">*</xref><xref ref-type="corresp" rid="cor1"><sup>¶</sup></xref></contrib><aff id="aff1">Cases *925 and</aff><aff id="aff2"><sup>§</sup>932, 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, 163 Avenue de Luminy, 13288 Marseille Cedex 9, France;</aff><aff id="aff3"><sup>†</sup>Centre for Cancer Research and Cell Biology, School of Biomedical Sciences, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom; and</aff><aff id="aff4"><sup>‡</sup>European Synchrotron Radiation Facility, ID23, B.P. 220, F-38043 Grenoble Cedex, France</aff></contrib-group><author-notes><corresp id="cor1"><sup>¶</sup>To whom correspondence should be addressed. E-mail:
<email>bruno.canard@afmb.univ-mrs.fr</email></corresp><fn fn-type="edited-by"><p>Edited by Charles M. Rice, The Rockefeller University, New York, NY, and approved June 23, 2006</p></fn><fn fn-type="con"><p>Author contributions: B. Canard designed research; S.R., M.-P.E., R.U., B. Coutard, and V.C. performed research; S.R., M.-P.E., R.U., D.N., C.C., J.Z., and B. Canard analyzed data; and S.R., C.C., J.Z., and B. Canard wrote the paper.</p></fn><fn fn-type="conflict"><p>Conflict of interest statement: No conflicts declared.</p></fn></author-notes><pub-date pub-type="ppub"><day>8</day><month>8</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>1</day><month>8</month><year>2006</year></pub-date><volume>103</volume><issue>32</issue><fpage>11892</fpage><lpage>11897</lpage><history><date date-type="received"><day>1</day><month>3</month><year>2006</year></date></history><copyright-statement>© 2006 by The National Academy of Sciences of the USA</copyright-statement><copyright-year>2006</copyright-year><self-uri xlink:title="pdf" xlink:href="zpq03206011892.pdf"></self-uri><abstract><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></abstract><kwd-group><kwd>endonuclease</kwd><kwd>severe acute respiratory syndrome</kwd><kwd>nidovirus</kwd><kwd>replication</kwd></kwd-group><custom-meta-wrap><custom-meta><meta-name>PDF</meta-name><meta-value><uri xlink:type="simple" xlink:href="zpq03206011892.pdf"></uri></meta-value></custom-meta></custom-meta-wrap></article-meta></front></pmc><affiliations><list><country><li>France</li><li>Royaume-Uni</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Provence-Alpes-Côte d'Azur</li><li>Rhône-Alpes</li></region><settlement><li>Grenoble</li><li>Marseille</li></settlement></list><tree><noCountry><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><name sortKey="Egloff, Marie Pierre" sort="Egloff, Marie Pierre" uniqKey="Egloff M" first="Marie-Pierre" last="Egloff">Marie-Pierre Egloff</name><name sortKey="Ricagno, Stefano" sort="Ricagno, Stefano" uniqKey="Ricagno S" first="Stefano" last="Ricagno">Stefano Ricagno</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Ulferts, Rachel" sort="Ulferts, Rachel" uniqKey="Ulferts R" first="Rachel" last="Ulferts">Rachel Ulferts</name></noRegion><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name></country><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Nurizzo, Didier" sort="Nurizzo, Didier" uniqKey="Nurizzo D" first="Didier" last="Nurizzo">Didier Nurizzo</name></region><name sortKey="Cambillau, Christian" sort="Cambillau, Christian" uniqKey="Cambillau C" first="Christian" last="Cambillau">Christian Cambillau</name><name sortKey="Campanacci, Valerie" sort="Campanacci, Valerie" uniqKey="Campanacci V" first="Valérie" last="Campanacci">Valérie Campanacci</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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