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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein</title><author><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><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichière">Julie Lichière</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Attoumani, Sarah" sort="Attoumani, Sarah" uniqKey="Attoumani S" first="Sarah" last="Attoumani">Sarah Attoumani</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">30644840</idno><idno type="pmc">7159728</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7159728</idno><idno type="RBID">PMC:7159728</idno><idno type="doi">10.1107/S2059798318014948</idno><date when="2019">2019</date><idno type="wicri:Area/Pmc/Corpus">000979</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000979</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein</title><author><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><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Lichiere, Julie" sort="Lichiere, Julie" uniqKey="Lichiere J" first="Julie" last="Lichière">Julie Lichière</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Papageorgiou, Nicolas" sort="Papageorgiou, Nicolas" uniqKey="Papageorgiou N" first="Nicolas" last="Papageorgiou">Nicolas Papageorgiou</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Attoumani, Sarah" sort="Attoumani, Sarah" uniqKey="Attoumani S" first="Sarah" last="Attoumani">Sarah Attoumani</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><affiliation><nlm:aff id="AYD2MN5116-aff-a1"></nlm:aff></affiliation><affiliation><nlm:aff id="AYD2MN5116-aff-a2"></nlm:aff></affiliation></author></analytic><series><title level="j">Acta Crystallographica. Section D, Structural Biology</title><idno type="eISSN">2059-7983</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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.</p></div></front></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Acta Crystallogr D Struct Biol</journal-id><journal-id journal-id-type="iso-abbrev">Acta Crystallogr D Struct Biol</journal-id><journal-id journal-id-type="doi">10.1107/S20597983</journal-id><journal-id journal-id-type="publisher-id">AYD2</journal-id><journal-title-group><journal-title>Acta Crystallographica. Section D, Structural Biology</journal-title></journal-title-group><issn pub-type="epub">2059-7983</issn><publisher><publisher-name>International Union of Crystallography</publisher-name><publisher-loc>5 Abbey Square, Chester, Cheshire CH1 2HU, England</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">30644840</article-id><article-id pub-id-type="pmc">7159728</article-id><article-id pub-id-type="doi">10.1107/S2059798318014948</article-id><article-id pub-id-type="publisher-id">AYD2MN5116</article-id><article-id pub-id-type="other">MN5116</article-id><article-categories><subj-group subj-group-type="overline"><subject>Research Papers</subject></subj-group><subj-group subj-group-type="heading"><subject>Research Papers</subject></subj-group></article-categories><title-group><article-title>Structure and oligomerization state of the C‐terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein</article-title><alt-title alt-title-type="right-running-head">C‐terminal region of the MERS‐CoV nucleoprotein</alt-title></title-group><contrib-group><contrib id="AYD2MN5116-cr-1" contrib-type="author"><name><surname>Nguyen</surname><given-names>Thi Hong Van</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref></contrib><contrib id="AYD2MN5116-cr-2" contrib-type="author"><name><surname>Lichière</surname><given-names>Julie</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref></contrib><contrib id="AYD2MN5116-cr-3" contrib-type="author"><name><surname>Canard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref></contrib><contrib id="AYD2MN5116-cr-4" contrib-type="author"><name><surname>Papageorgiou</surname><given-names>Nicolas</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref></contrib><contrib id="AYD2MN5116-cr-5" contrib-type="author"><name><surname>Attoumani</surname><given-names>Sarah</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref></contrib><contrib id="AYD2MN5116-cr-6" contrib-type="author" corresp="yes"><name><surname>Ferron</surname><given-names>François</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref><address><email>francois.ferron@afmb.univ-mrs.fr</email></address></contrib><contrib id="AYD2MN5116-cr-7" contrib-type="author" corresp="yes"><name><surname>Coutard</surname><given-names>Bruno</given-names></name><xref ref-type="aff" rid="AYD2MN5116-aff-a1"><sup>1</sup></xref><xref ref-type="aff" rid="AYD2MN5116-aff-a2"><sup>2</sup></xref><address><email>bruno.coutard@afmb.univ-mrs.fr</email></address></contrib></contrib-group><aff id="AYD2MN5116-aff-a1"><label><sup>1</sup></label>Aix-Marseille Université, AFMB UMR 7257, 13288Marseilles, France</aff><aff id="AYD2MN5116-aff-a2"><label><sup>2</sup></label>CNRS, AFMB UMR 7257, 13288Marseilles, France</aff><author-notes><corresp id="correspondenceTo"><label>*</label>François Ferron, e-mail: <email>francois.ferron@afmb.univ-mrs.fr</email>; Bruno Coutard, e-mail: <email>bruno.coutard@afmb.univ-mrs.fr</email></corresp></author-notes><pub-date pub-type="epub"><day>15</day><month>1</month><year>2019</year></pub-date><pub-date pub-type="ppub"><month>1</month><year>2019</year></pub-date><volume>75</volume><issue>1</issue><issue-id pub-id-type="doi">10.1107/S20597983750100</issue-id><fpage>8</fpage><lpage>15</lpage><history><date date-type="received"><day>11</day><month>7</month><year>2018</year></date><date date-type="accepted"><day>22</day><month>10</month><year>2018</year></date></history><permissions><copyright-statement content-type="article-copyright">© International Union of Crystallography, 2019</copyright-statement><license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:AYD2-75-8.pdf"></self-uri><abstract><p>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.</p></abstract><abstract abstract-type="graphical"><p>The X‐ray structure and SAXS analysis of the C‐terminal domain of the nucleocapsid from Middle East respiratory syndrome coronavirus, an emerging virus, are reported.<boxed-text position="anchor" content-type="graphic" orientation="portrait"><graphic xlink:href="AYD2-75-8-g001.jpg" position="anchor" id="nlm-graphic-1" orientation="portrait"></graphic></boxed-text></p></abstract><kwd-group><kwd id="AYD2MN5116-kwd-1">nucleoproteins</kwd><kwd id="AYD2MN5116-kwd-2">Middle East respiratory syndrome coronavirus</kwd><kwd id="AYD2MN5116-kwd-3">MERS‐CoV</kwd><kwd id="AYD2MN5116-kwd-4"><italic>Coronaviridae</italic></kwd><kwd id="AYD2MN5116-kwd-5">X‐ray diffraction</kwd><kwd id="AYD2MN5116-kwd-6">SAXS</kwd></kwd-group><counts><fig-count count="0"></fig-count><table-count count="0"></table-count><page-count count="7"></page-count><word-count count="0"></word-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>January 2019</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front><body><p>The full text for this article, hosted at <ext-link ext-link-type="uri" xlink:href="http://journals.iucr.org">http://journals.iucr.org</ext-link>, is unavailable due to technical difficulties.</p><sec sec-type="supplementary-material"><title>Supporting information</title><supplementary-material content-type="local-data"><p>Supporting information for this article can be found <ext-link ext-link-type="uri" xlink:href="http://scripts.iucr.org/cgi-bin/paper?mn5116">http://scripts.iucr.org/cgi-bin/paper?mn5116</ext-link></p></supplementary-material></sec></body></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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