Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Identifieur interne : 001490 ( Ncbi/Merge ); précédent : 001489; suivant : 001491Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Auteurs : Nicolas Papageorgiou ; Julie Lichière ; Amal Baklouti ; François Ferron ; Marion Sévajol ; Bruno Canard ; Bruno CoutardSource :
- Acta Crystallographica. Section D, Structural Biology [ 2059-7983 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- Crystallization, Crystallography, X-Ray, Models, Molecular, Protein Multimerization, Protein Structure, Tertiary, Scattering, Small Angle.
Abstract
The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N‐terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N‐terminal domain (NTD). In this study, the structure determination of the N‐terminal region of the MERS‐CoV N protein
Url:
DOI: 10.1107/S2059798315024328
PubMed: 26894667
PubMed Central: 7159594
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PMC:7159594Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N‐terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N‐terminal domain (NTD). In this study, the structure determination of the N‐terminal region of the MERS‐CoV N protein <italic>via</italic>
X‐ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X‐ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N‐terminal region of the MERS‐CoV as a monomer that displays structural features in common with other coronavirus NTDs.</p>
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X‐ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X‐ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N‐terminal region of the MERS‐CoV as a monomer that displays structural features in common with other coronavirus NTDs.</p>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.</title>
<author><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichière">Julie Lichière</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Baklouti, Amal" sort="Baklouti, Amal" uniqKey="Baklouti A" first="Amal" last="Baklouti">Amal Baklouti</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Sevajol, Marion" sort="Sevajol, Marion" uniqKey="Sevajol M" first="Marion" last="Sévajol">Marion Sévajol</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</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="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name>
<affiliation wicri:level="3"><nlm:affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>CNRS, AFMB UMR 7257, 13288 Marseille</wicri:regionArea>
<placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region>
<settlement type="city">Marseille</settlement>
</placeName>
</affiliation>
</author>
</analytic>
<series><title level="j">Acta crystallographica. Section D, Structural biology</title>
<idno type="eISSN">2059-7983</idno>
<imprint><date when="2016" type="published">2016</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization</term>
<term>Crystallography, X-Ray</term>
<term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term>
<term>Models, Molecular</term>
<term>Nucleocapsid Proteins (chemistry)</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Tertiary</term>
<term>Scattering, Small Angle</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term>
<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
<term>Diffusion aux petits angles</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Protéines nucléocapside ()</term>
<term>Structure tertiaire des protéines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Crystallization</term>
<term>Crystallography, X-Ray</term>
<term>Models, Molecular</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Tertiary</term>
<term>Scattering, Small Angle</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Cristallisation</term>
<term>Cristallographie aux rayons X</term>
<term>Diffusion aux petits angles</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Protéines nucléocapside</term>
<term>Structure tertiaire des protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N-terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N-terminal domain (NTD). In this study, the structure determination of the N-terminal region of the MERS-CoV N protein via X-ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X-ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N-terminal region of the MERS-CoV as a monomer that displays structural features in common with other coronavirus NTDs. </div>
</front>
</TEI>
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