Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein
Identifieur interne : 000367 ( Main/Exploration ); précédent : 000366; suivant : 000368Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein
Auteurs : Thi Hong Van Nguyen ; Julie Lichière ; Bruno Canard ; Nicolas Papageorgiou ; Sarah Attoumani ; François Ferron ; Bruno CoutardSource :
- Acta Crystallographica. Section D, Structural Biology [ 2059-7983 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Nucleoproteins, Viral Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- Humans, Molecular Structure, Protein Multimerization, Scattering, Small Angle, Static Electricity, X-Ray Diffraction.
Abstract
Middle East respiratory syndrome coronavirus (MERS‐CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C‐terminal domain of N from MERS‐CoV obtained using single‐crystal X‐ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small‐angle X‐ray scattering measurements. Comparisons with the structures of the C‐terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.
Url:
DOI: 10.1107/S2059798318014948
PubMed: 30644840
PubMed Central: 7159728
Affiliations:
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Le document en format XML
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Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C‐terminal domain of N from MERS‐CoV obtained using single‐crystal X‐ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small‐angle X‐ray scattering measurements. Comparisons with the structures of the C‐terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Attoumani, Sarah" sort="Attoumani, Sarah" uniqKey="Attoumani S" first="Sarah" last="Attoumani">Sarah Attoumani</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="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichière">Julie Lichière</name><name sortKey="Nguyen, Thi Hong Van" sort="Nguyen, Thi Hong Van" uniqKey="Nguyen T" first="Thi Hong Van" last="Nguyen">Thi Hong Van Nguyen</name><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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