Crystal structure of Middle East respiratory syndrome coronavirus helicase
Identifieur interne : 000E40 ( Main/Exploration ); précédent : 000E39; suivant : 000E41Crystal structure of Middle East respiratory syndrome coronavirus helicase
Auteurs : Wei Hao [République populaire de Chine] ; Justyna Aleksandra Wojdyla [Suisse] ; Rong Zhao [République populaire de Chine] ; Ruiyun Han [République populaire de Chine] ; Rajat Das [États-Unis] ; Ivan Zlatev [États-Unis] ; Muthiah Manoharan [États-Unis] ; Meitian Wang [Suisse] ; Sheng Cui [République populaire de Chine]Source :
- PLoS Pathogens [ 1553-7366 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Coronavirus du syndrome respiratoire du Moyen-Orient.
- métabolisme : Helicase.
- virologie : Infections à coronavirus.
- Helicase, Humains, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Structure secondaire des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : DNA Helicases.
- chemical , metabolism : DNA Helicases.
- enzymology : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Humans, Models, Molecular, Protein Interaction Domains and Motifs, Protein Structure, Secondary.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.
Url:
DOI: 10.1371/journal.ppat.1006474
PubMed: 28651017
PubMed Central: 5501694
Affiliations:
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Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing, China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Han, Ruiyun" sort="Han, Ruiyun" uniqKey="Han R" first="Ruiyun" last="Han">Ruiyun Han</name><affiliation wicri:level="3"><nlm:aff id="aff001"><addr-line>MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing, China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Das, Rajat" sort="Das, Rajat" uniqKey="Das R" first="Rajat" last="Das">Rajat Das</name><affiliation wicri:level="2"><nlm:aff id="aff003"><addr-line>Alnylam Pharmaceuticals, Cambridge, MA, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Alnylam Pharmaceuticals, Cambridge, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Zlatev, Ivan" sort="Zlatev, Ivan" uniqKey="Zlatev I" first="Ivan" last="Zlatev">Ivan Zlatev</name><affiliation wicri:level="2"><nlm:aff id="aff003"><addr-line>Alnylam Pharmaceuticals, Cambridge, MA, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Alnylam Pharmaceuticals, Cambridge, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Manoharan, Muthiah" sort="Manoharan, Muthiah" uniqKey="Manoharan M" first="Muthiah" last="Manoharan">Muthiah Manoharan</name><affiliation wicri:level="2"><nlm:aff id="aff003"><addr-line>Alnylam Pharmaceuticals, Cambridge, MA, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Alnylam Pharmaceuticals, Cambridge, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Wang, Meitian" sort="Wang, Meitian" uniqKey="Wang M" first="Meitian" last="Wang">Meitian Wang</name><affiliation wicri:level="1"><nlm:aff id="aff002"><addr-line>Swiss Light Source at Paul Scherrer Institute, Villigen, Switzerland</addr-line></nlm:aff><country xml:lang="fr">Suisse</country><wicri:regionArea>Swiss Light Source at Paul Scherrer Institute, Villigen</wicri:regionArea><wicri:noRegion>Villigen</wicri:noRegion></affiliation></author><author><name sortKey="Cui, Sheng" sort="Cui, Sheng" uniqKey="Cui S" first="Sheng" last="Cui">Sheng Cui</name><affiliation wicri:level="3"><nlm:aff id="aff001"><addr-line>MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing, China</addr-line></nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></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="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus Infections (virology)</term><term>DNA Helicases (chemistry)</term><term>DNA Helicases (metabolism)</term><term>Humans</term><term>Middle East Respiratory Syndrome Coronavirus (enzymology)</term><term>Models, Molecular</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie)</term><term>Helicase ()</term><term>Helicase (métabolisme)</term><term>Humains</term><term>Infections à coronavirus (virologie)</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Structure secondaire des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA Helicases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Helicases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Helicase</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Models, Molecular</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Helicase</term><term>Humains</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Stadler, K" uniqKey="Stadler K">K Stadler</name></author><author><name sortKey="Masignani, V" uniqKey="Masignani V">V Masignani</name></author><author><name sortKey="Eickmann, M" uniqKey="Eickmann M">M Eickmann</name></author><author><name sortKey="Becker, S" uniqKey="Becker S">S Becker</name></author><author><name sortKey="Abrignani, S" uniqKey="Abrignani S">S Abrignani</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zaki, Am" uniqKey="Zaki A">AM Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S van Boheemen</name></author><author><name sortKey="Bestebroer, Tm" uniqKey="Bestebroer T">TM Bestebroer</name></author><author><name sortKey="Osterhaus, Ad" uniqKey="Osterhaus A">AD Osterhaus</name></author><author><name sortKey="Fouchier, Ra" uniqKey="Fouchier R">RA Fouchier</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kupferschmidt, K" uniqKey="Kupferschmidt K">K Kupferschmidt</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gorbalenya, Ae" uniqKey="Gorbalenya A">AE Gorbalenya</name></author><author><name sortKey="Enjuanes, L" uniqKey="Enjuanes L">L Enjuanes</name></author><author><name sortKey="Ziebuhr, J" uniqKey="Ziebuhr J">J Ziebuhr</name></author><author><name sortKey="Snijder, Ej" uniqKey="Snijder E">EJ Snijder</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="De Groot, Rj" uniqKey="De Groot R">RJ de Groot</name></author><author><name sortKey="Cowley, J A" uniqKey="Cowley J">J.A. 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uniqKey="Han R" first="Ruiyun" last="Han">Ruiyun Han</name><name sortKey="Zhao, Rong" sort="Zhao, Rong" uniqKey="Zhao R" first="Rong" last="Zhao">Rong Zhao</name></country><country name="Suisse"><noRegion><name sortKey="Wojdyla, Justyna Aleksandra" sort="Wojdyla, Justyna Aleksandra" uniqKey="Wojdyla J" first="Justyna Aleksandra" last="Wojdyla">Justyna Aleksandra Wojdyla</name></noRegion><name sortKey="Wang, Meitian" sort="Wang, Meitian" uniqKey="Wang M" first="Meitian" last="Wang">Meitian Wang</name></country><country name="États-Unis"><region name="Massachusetts"><name sortKey="Das, Rajat" sort="Das, Rajat" uniqKey="Das R" first="Rajat" last="Das">Rajat Das</name></region><name sortKey="Manoharan, Muthiah" sort="Manoharan, Muthiah" uniqKey="Manoharan M" first="Muthiah" last="Manoharan">Muthiah Manoharan</name><name sortKey="Zlatev, Ivan" sort="Zlatev, Ivan" uniqKey="Zlatev I" first="Ivan" last="Zlatev">Ivan Zlatev</name></country></tree></affiliations></record>Pour manipuler ce 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