Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.
Identifieur interne : 000674 ( PubMed/Curation ); précédent : 000673; suivant : 000675Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.
Auteurs : Thi Hong Van Nguyen [France] ; Julie Lichière [France] ; Bruno Canard [France] ; Nicolas Papageorgiou [France] ; Sarah Attoumani [France] ; François Ferron [France] ; Bruno Coutard [France]Source :
- 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.
DOI: 10.1107/S2059798318014948
PubMed: 30644840
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30644840</PMID><DateCompleted><Year>2019</Year><Month>05</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2059-7983</ISSN><JournalIssue CitedMedium="Internet"><Volume>75</Volume><Issue>Pt 1</Issue><PubDate><Year>2019</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Structural biology</Title><ISOAbbreviation>Acta Crystallogr D Struct Biol</ISOAbbreviation></Journal><ArticleTitle>Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.</ArticleTitle><Pagination><MedlinePgn>8-15</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S2059798318014948</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nguyen</LastName><ForeName>Thi Hong Van</ForeName><Initials>THV</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lichière</LastName><ForeName>Julie</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Papageorgiou</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Attoumani</LastName><ForeName>Sarah</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferron</LastName><ForeName>François</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0002-8351-4992</Identifier><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Aix-Marseille Université, AFMB UMR 7257, 13288 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