Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Identifieur interne : 001251 ( PubMed/Curation ); précédent : 001250; suivant : 001252Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.
Auteurs : Nicolas Papageorgiou [France] ; Julie Lichière [France] ; Amal Baklouti [France] ; François Ferron [France] ; Marion Sévajol [France] ; Bruno Canard [France] ; Bruno Coutard [France]Source :
- 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 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.
DOI: 10.1107/S2059798315024328
PubMed: 26894667
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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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26894667</PMID><DateCompleted><Year>2016</Year><Month>11</Month><Day>11</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>72</Volume><Issue>Pt 2</Issue><PubDate><Year>2016</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Structural biology</Title><ISOAbbreviation>Acta Crystallogr D Struct Biol</ISOAbbreviation></Journal><ArticleTitle>Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering.</ArticleTitle><Pagination><MedlinePgn>192-202</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S2059798315024328</ELocationID><Abstract><AbstractText>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. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Papageorgiou</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lichière</LastName><ForeName>Julie</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baklouti</LastName><ForeName>Amal</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferron</LastName><ForeName>François</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sévajol</LastName><ForeName>Marion</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>01</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Struct Biol</MedlineTA><NlmUniqueID>101676043</NlmUniqueID><ISSNLinking>2059-7983</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003460" MajorTopicYN="N">Crystallization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053838" MajorTopicYN="N">Scattering, Small Angle</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">MERS-CoV</Keyword><Keyword MajorTopicYN="N">RNA-binding domain</Keyword><Keyword MajorTopicYN="N">SAXS</Keyword><Keyword MajorTopicYN="N">nucleocapsid</Keyword><Keyword MajorTopicYN="N">structure</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>10</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>12</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>2</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>2</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26894667</ArticleId><ArticleId IdType="pii">S2059798315024328</ArticleId><ArticleId IdType="doi">10.1107/S2059798315024328</ArticleId><ArticleId IdType="pmc">PMC7159594</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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