SrasV1, France, Analysis, bibRecord, 000195

Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex

Identifieur interne : 000195 ( France/Analysis ); précédent : 000194; suivant : 000196

Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex

Auteurs : Etienne Decroly [France] ; Claire Debarnot [France] ; François Ferron [France] ; Mickael Bouvet [France] ; Bruno Coutard [France] ; Isabelle Imbert [France] ; Laure Gluais [France] ; Nicolas Papageorgiou [France] ; Andrew Sharff [Royaume-Uni] ; Gérard Bricogne [Royaume-Uni] ; Miguel Ortiz-Lombardia [France] ; Julien Lescar [France] ; Bruno Canard [France]

Source :

PLoS Pathogens [ 1553-7366 ] ; 2011.

RBID : PMC:3102710

Descripteurs français

KwdFr :
- ARN viral (métabolisme), Adémétionine (métabolisme), Adénosine (analogues et dérivés), Adénosine (métabolisme), Coiffes des ARN (métabolisme), Cristallisation, Liaison aux protéines, Magnésium (métabolisme), Methyltransferases (), Methyltransferases (métabolisme), Mutation (génétique), Plasmides, Protéines virales non structurales (), Protéines virales non structurales (métabolisme), Virus du SRAS (génétique).
MESH :
- analogues et dérivés : Adénosine.
- génétique : Mutation, Virus du SRAS.
- métabolisme : ARN viral, Adémétionine, Adénosine, Coiffes des ARN, Magnésium, Methyltransferases, Protéines virales non structurales.
- Cristallisation, Liaison aux protéines, Methyltransferases, Plasmides, Protéines virales non structurales.

English descriptors

KwdEn :
- Adenosine (analogs & derivatives), Adenosine (metabolism), Crystallization, Magnesium (metabolism), Methyltransferases (chemistry), Methyltransferases (metabolism), Mutation (genetics), Plasmids, Protein Binding, RNA Caps (metabolism), RNA, Viral (metabolism), S-Adenosylmethionine (metabolism), SARS Virus (genetics), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , analogs & derivatives : Adenosine.
- chemical , chemistry : Methyltransferases, Viral Nonstructural Proteins.
- chemical , metabolism : Adenosine, Magnesium, Methyltransferases, RNA Caps, RNA, Viral, S-Adenosylmethionine, Viral Nonstructural Proteins.
- genetics : Mutation, SARS Virus.
- Crystallization, Plasmids, Protein Binding.

Abstract

Cellular and viral S-adenosylmethionine-dependent methyltransferases are involved in many regulated processes such as metabolism, detoxification, signal transduction, chromatin remodeling, nucleic acid processing, and mRNA capping. The Severe Acute Respiratory Syndrome coronavirus nsp16 protein is a S-adenosylmethionine-dependent (nucleoside-2′-O)-methyltransferase only active in the presence of its activating partner nsp10. We report the nsp10/nsp16 complex structure at 2.0 Å resolution, which shows nsp10 bound to nsp16 through a ∼930 Å² surface area in nsp10. Functional assays identify key residues involved in nsp10/nsp16 association, and in RNA binding or catalysis, the latter likely through a SN2-like mechanism. We present two other crystal structures, the inhibitor Sinefungin bound in the S-adenosylmethionine binding pocket and the tighter complex nsp10(Y96F)/nsp16, providing the first structural insight into the regulation of RNA capping enzymes in (+)RNA viruses.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3102710

DOI: 10.1371/journal.ppat.1002059
PubMed: 21637813
PubMed Central: 3102710

Affiliations:

Links to Exploration step

PMC:3102710

Le document en format XML

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<author><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name>
<affiliation wicri:level="4"><nlm:aff id="aff1"><addr-line>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France</addr-line>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille</wicri:regionArea>
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<settlement type="city">Marseille</settlement>
</placeName>
<orgName type="university">Université de la Méditerranée</orgName>
</affiliation>
</author>
<author><name sortKey="Sharff, Andrew" sort="Sharff, Andrew" uniqKey="Sharff A" first="Andrew" last="Sharff">Andrew Sharff</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Global Phasing Ltd., Sheraton House, Castle Park, Cambridge, United Kingdom</addr-line>
</nlm:aff>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Global Phasing Ltd., Sheraton House, Castle Park, Cambridge</wicri:regionArea>
<wicri:noRegion>Cambridge</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Bricogne, Gerard" sort="Bricogne, Gerard" uniqKey="Bricogne G" first="Gérard" last="Bricogne">Gérard Bricogne</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"><addr-line>Global Phasing Ltd., Sheraton House, Castle Park, Cambridge, United Kingdom</addr-line>
</nlm:aff>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Global Phasing Ltd., Sheraton House, Castle Park, Cambridge</wicri:regionArea>
<wicri:noRegion>Cambridge</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Ortiz Lombardia, Miguel" sort="Ortiz Lombardia, Miguel" uniqKey="Ortiz Lombardia M" first="Miguel" last="Ortiz-Lombardia">Miguel Ortiz-Lombardia</name>
<affiliation wicri:level="4"><nlm:aff id="aff1"><addr-line>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France</addr-line>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille</wicri:regionArea>
<placeName><region type="region">Provence-Alpes-Côte d'Azur</region>
<region type="old region">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Marseille</settlement>
</placeName>
<orgName type="university">Université de la Méditerranée</orgName>
</affiliation>
</author>
<author><name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</name>
<affiliation wicri:level="4"><nlm:aff id="aff1"><addr-line>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France</addr-line>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille</wicri:regionArea>
<placeName><region type="region">Provence-Alpes-Côte d'Azur</region>
<region type="old region">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Marseille</settlement>
</placeName>
<orgName type="university">Université de la Méditerranée</orgName>
</affiliation>
<affiliation><nlm:aff id="aff3"><addr-line>School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore</addr-line>
</nlm:aff>
<wicri:noCountry code="subfield">Republic of Singapore</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name>
<affiliation wicri:level="4"><nlm:aff id="aff1"><addr-line>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France</addr-line>
</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille</wicri:regionArea>
<placeName><region type="region">Provence-Alpes-Côte d'Azur</region>
<region type="old region">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Marseille</settlement>
</placeName>
<orgName type="university">Université de la Méditerranée</orgName>
</affiliation>
</author>
</analytic>
<series><title level="j">PLoS Pathogens</title>
<idno type="ISSN">1553-7366</idno>
<idno type="eISSN">1553-7374</idno>
<imprint><date when="2011">2011</date>
</imprint>
</series>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine (analogs & derivatives)</term>
<term>Adenosine (metabolism)</term>
<term>Crystallization</term>
<term>Magnesium (metabolism)</term>
<term>Methyltransferases (chemistry)</term>
<term>Methyltransferases (metabolism)</term>
<term>Mutation (genetics)</term>
<term>Plasmids</term>
<term>Protein Binding</term>
<term>RNA Caps (metabolism)</term>
<term>RNA, Viral (metabolism)</term>
<term>S-Adenosylmethionine (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ARN viral (métabolisme)</term>
<term>Adémétionine (métabolisme)</term>
<term>Adénosine (analogues et dérivés)</term>
<term>Adénosine (métabolisme)</term>
<term>Coiffes des ARN (métabolisme)</term>
<term>Cristallisation</term>
<term>Liaison aux protéines</term>
<term>Magnésium (métabolisme)</term>
<term>Methyltransferases ()</term>
<term>Methyltransferases (métabolisme)</term>
<term>Mutation (génétique)</term>
<term>Plasmides</term>
<term>Protéines virales non structurales ()</term>
<term>Protéines virales non structurales (métabolisme)</term>
<term>Virus du SRAS (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Adenosine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Methyltransferases</term>
<term>Viral Nonstructural Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine</term>
<term>Magnesium</term>
<term>Methyltransferases</term>
<term>RNA Caps</term>
<term>RNA, Viral</term>
<term>S-Adenosylmethionine</term>
<term>Viral Nonstructural Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Adénosine</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN viral</term>
<term>Adémétionine</term>
<term>Adénosine</term>
<term>Coiffes des ARN</term>
<term>Magnésium</term>
<term>Methyltransferases</term>
<term>Protéines virales non structurales</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Crystallization</term>
<term>Plasmids</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cristallisation</term>
<term>Liaison aux protéines</term>
<term>Methyltransferases</term>
<term>Plasmides</term>
<term>Protéines virales non structurales</term>
</keywords>
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<front><div type="abstract" xml:lang="en"><p>Cellular and viral S-adenosylmethionine-dependent methyltransferases are involved in many regulated processes such as metabolism, detoxification, signal transduction, chromatin remodeling, nucleic acid processing, and mRNA capping. The Severe Acute Respiratory Syndrome coronavirus nsp16 protein is a S-adenosylmethionine-dependent (nucleoside-2′-O)-methyltransferase only active in the presence of its activating partner nsp10. We report the nsp10/nsp16 complex structure at 2.0 Å resolution, which shows nsp10 bound to nsp16 through a ∼930 Å<sup>2</sup>
 surface area in nsp10. Functional assays identify key residues involved in nsp10/nsp16 association, and in RNA binding or catalysis, the latter likely through a SN2-like mechanism. We present two other crystal structures, the inhibitor Sinefungin bound in the S-adenosylmethionine binding pocket and the tighter complex nsp10(Y96F)/nsp16, providing the first structural insight into the regulation of RNA capping enzymes in (+)RNA viruses.</p>
</div>
</front>
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<author><name sortKey="Thiel, V" uniqKey="Thiel V">V Thiel</name>
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<author><name sortKey="Ziebuhr, J" uniqKey="Ziebuhr J">J Ziebuhr</name>
</author>
</analytic>
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</author>
<author><name sortKey="De Clercq, E" uniqKey="De Clercq E">E De Clercq</name>
</author>
<author><name sortKey="Serafinowski, P" uniqKey="Serafinowski P">P Serafinowski</name>
</author>
<author><name sortKey="Dorland, E" uniqKey="Dorland E">E Dorland</name>
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</author>
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</author>
</analytic>
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<author><name sortKey="Borchardt, Rt" uniqKey="Borchardt R">RT Borchardt</name>
</author>
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<author><name sortKey="Ferron, F" uniqKey="Ferron F">F Ferron</name>
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<author><name sortKey="Gluais, L" uniqKey="Gluais L">L Gluais</name>
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<author><name sortKey="Sonenberg, N" uniqKey="Sonenberg N">N Sonenberg</name>
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<author><name sortKey="Resa Infante, P" uniqKey="Resa Infante P">P Resa-Infante</name>
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<author><name sortKey="Shinobu, N" uniqKey="Shinobu N">N Shinobu</name>
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</analytic>
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<author><name sortKey="Selisko, B" uniqKey="Selisko B">B Selisko</name>
</author>
<author><name sortKey="Decroly, E" uniqKey="Decroly E">E Decroly</name>
</author>
<author><name sortKey="Vasseur, Jj" uniqKey="Vasseur J">JJ Vasseur</name>
</author>
<author><name sortKey="Benarroch, D" uniqKey="Benarroch D">D Benarroch</name>
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</div1>
</back>
</TEI>
<affiliations><list><country><li>France</li>
<li>Royaume-Uni</li>
</country>
<region><li>Provence-Alpes-Côte d'Azur</li>
</region>
<settlement><li>Marseille</li>
</settlement>
<orgName><li>Université de la Méditerranée</li>
</orgName>
</list>
<tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Decroly, Etienne" sort="Decroly, Etienne" uniqKey="Decroly E" first="Etienne" last="Decroly">Etienne Decroly</name>
</region>
<name sortKey="Bouvet, Mickael" sort="Bouvet, Mickael" uniqKey="Bouvet M" first="Mickael" last="Bouvet">Mickael Bouvet</name>
<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="Debarnot, Claire" sort="Debarnot, Claire" uniqKey="Debarnot C" first="Claire" last="Debarnot">Claire Debarnot</name>
<name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name>
<name sortKey="Gluais, Laure" sort="Gluais, Laure" uniqKey="Gluais L" first="Laure" last="Gluais">Laure Gluais</name>
<name sortKey="Imbert, Isabelle" sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name>
<name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</name>
<name sortKey="Ortiz Lombardia, Miguel" sort="Ortiz Lombardia, Miguel" uniqKey="Ortiz Lombardia M" first="Miguel" last="Ortiz-Lombardia">Miguel Ortiz-Lombardia</name>
<name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name>
</country>
<country name="Royaume-Uni"><noRegion><name sortKey="Sharff, Andrew" sort="Sharff, Andrew" uniqKey="Sharff A" first="Andrew" last="Sharff">Andrew Sharff</name>
</noRegion>
<name sortKey="Bricogne, Gerard" sort="Bricogne, Gerard" uniqKey="Bricogne G" first="Gérard" last="Bricogne">Gérard Bricogne</name>
</country>
</tree>
</affiliations>
</record>

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   |texte=   Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex
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Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex

Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 Complex

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