Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex.
Identifieur interne : 001505 ( PubMed/Corpus ); précédent : 001504; suivant : 001506Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex.
Auteurs : Etienne Decroly ; Claire Debarnot ; François Ferron ; Mickael Bouvet ; Bruno Coutard ; Isabelle Imbert ; Laure Gluais ; Nicolas Papageorgiou ; Andrew Sharff ; Gérard Bricogne ; Miguel Ortiz-Lombardia ; Julien Lescar ; Bruno CanardSource :
- PLoS pathogens [ 1553-7374 ] ; 2011.
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 Ų 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.
DOI: 10.1371/journal.ppat.1002059
PubMed: 21637813
Links to Exploration step
pubmed:21637813Le document en format XML
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sort="Decroly, Etienne" uniqKey="Decroly E" first="Etienne" last="Decroly">Etienne Decroly</name><affiliation><nlm:affiliation>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France. etienne.decroly@afmb.univ-mrs.fr</nlm:affiliation></affiliation></author><author><name sortKey="Debarnot, Claire" sort="Debarnot, Claire" uniqKey="Debarnot C" first="Claire" last="Debarnot">Claire Debarnot</name></author><author><name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name></author><author><name sortKey="Bouvet, Mickael" sort="Bouvet, Mickael" uniqKey="Bouvet M" first="Mickael" last="Bouvet">Mickael Bouvet</name></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name></author><author><name sortKey="Imbert, Isabelle" sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name></author><author><name sortKey="Gluais, Laure" sort="Gluais, Laure" uniqKey="Gluais L" first="Laure" last="Gluais">Laure Gluais</name></author><author><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name></author><author><name sortKey="Sharff, Andrew" sort="Sharff, Andrew" uniqKey="Sharff A" first="Andrew" last="Sharff">Andrew Sharff</name></author><author><name sortKey="Bricogne, Gerard" sort="Bricogne, Gerard" uniqKey="Bricogne G" first="Gérard" last="Bricogne">Gérard Bricogne</name></author><author><name sortKey="Ortiz Lombardia, Miguel" sort="Ortiz Lombardia, Miguel" uniqKey="Ortiz Lombardia M" first="Miguel" last="Ortiz-Lombardia">Miguel Ortiz-Lombardia</name></author><author><name sortKey="Lescar, Julien" sort="Lescar, Julien" uniqKey="Lescar J" first="Julien" last="Lescar">Julien Lescar</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">PLoS pathogens</title><idno type="eISSN">1553-7374</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><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="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="genetics" xml:lang="en"><term>Mutation</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallization</term><term>Plasmids</term><term>Protein Binding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 Ų 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21637813</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1553-7374</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>5</Issue><PubDate><Year>2011</Year><Month>May</Month></PubDate></JournalIssue><Title>PLoS pathogens</Title><ISOAbbreviation>PLoS Pathog.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure and functional analysis of the SARS-coronavirus RNA cap 2'-O-methyltransferase nsp10/nsp16 complex.</ArticleTitle><Pagination><MedlinePgn>e1002059</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.ppat.1002059</ELocationID><Abstract><AbstractText>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 Ų 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Decroly</LastName><ForeName>Etienne</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Centre National de la Recherche Scientifique and Université de la Méditerranée, UMR 6098, Architecture et Fonction des Macromolécules Biologiques, Marseille, France. etienne.decroly@afmb.univ-mrs.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Debarnot</LastName><ForeName>Claire</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Ferron</LastName><ForeName>François</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Bouvet</LastName><ForeName>Mickael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Imbert</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Gluais</LastName><ForeName>Laure</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Papageorgiou</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Sharff</LastName><ForeName>Andrew</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Bricogne</LastName><ForeName>Gérard</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Ortiz-Lombardia</LastName><ForeName>Miguel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Lescar</LastName><ForeName>Julien</ForeName><Initials>J</Initials></Author><Author 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