Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering
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‐term...
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| Veröffentlicht in: | Acta crystallographica. Section D, Structural biology Structural biology, 2016-02, Vol.72 (2), p.192-202 |
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| container_title | Acta crystallographica. Section D, Structural biology |
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| creator | Papageorgiou, Nicolas Lichière, Julie Baklouti, Amal Ferron, François Sévajol, Marion Canard, Bruno Coutard, Bruno |
| description | 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.
The structural characterization of the N‐terminal part of the nucleocapsid from Middle East respiratory syndrome coronavirus (MERS‐CoV), a recently emerging virus, is reported. The structure of the N‐terminal region, which includes a disordered tail followed by a globular domain, was obtained by combining X‐ray diffraction and SAXS. |
| doi_str_mv | 10.1107/S2059798315024328 |
| format | Article |
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The structural characterization of the N‐terminal part of the nucleocapsid from Middle East respiratory syndrome coronavirus (MERS‐CoV), a recently emerging virus, is reported. The structure of the N‐terminal region, which includes a disordered tail followed by a globular domain, was obtained by combining X‐ray diffraction and SAXS.</description><identifier>ISSN: 2059-7983</identifier><identifier>EISSN: 2059-7983</identifier><identifier>DOI: 10.1107/S2059798315024328</identifier><identifier>PMID: 26894667</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Biochemistry, Molecular Biology ; Crystallization ; Crystallography, X-Ray ; Life Sciences ; MERS-CoV ; Middle East Respiratory Syndrome Coronavirus - chemistry ; Models, Molecular ; nucleocapsid ; Nucleocapsid Proteins - chemistry ; Protein Multimerization ; Protein Structure, Tertiary ; Quantitative Methods ; Research Papers ; RNA-binding domain ; SAXS ; Scattering, Small Angle ; Structural Biology ; structure</subject><ispartof>Acta crystallographica. Section D, Structural biology, 2016-02, Vol.72 (2), p.192-202</ispartof><rights>International Union of Crystallography, 2016</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5215-fed7be956ce812839321ed86ae534a9ae70d37687c110517157f4de4a56adbf3</citedby><cites>FETCH-LOGICAL-c5215-fed7be956ce812839321ed86ae534a9ae70d37687c110517157f4de4a56adbf3</cites><orcidid>0000-0002-8351-4992 ; 0000-0002-2859-7123 ; 0000-0003-4924-1991</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1107%2FS2059798315024328$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1107%2FS2059798315024328$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,315,782,786,887,1419,27931,27932,45581,45582</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26894667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01439080$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Papageorgiou, Nicolas</creatorcontrib><creatorcontrib>Lichière, Julie</creatorcontrib><creatorcontrib>Baklouti, Amal</creatorcontrib><creatorcontrib>Ferron, François</creatorcontrib><creatorcontrib>Sévajol, Marion</creatorcontrib><creatorcontrib>Canard, Bruno</creatorcontrib><creatorcontrib>Coutard, Bruno</creatorcontrib><title>Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering</title><title>Acta crystallographica. Section D, Structural biology</title><addtitle>Acta Cryst. D</addtitle><description>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.
The structural characterization of the N‐terminal part of the nucleocapsid from Middle East respiratory syndrome coronavirus (MERS‐CoV), a recently emerging virus, is reported. The structure of the N‐terminal region, which includes a disordered tail followed by a globular domain, was obtained by combining X‐ray diffraction and SAXS.</description><subject>Biochemistry, Molecular Biology</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Life Sciences</subject><subject>MERS-CoV</subject><subject>Middle East Respiratory Syndrome Coronavirus - chemistry</subject><subject>Models, Molecular</subject><subject>nucleocapsid</subject><subject>Nucleocapsid Proteins - chemistry</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Tertiary</subject><subject>Quantitative Methods</subject><subject>Research Papers</subject><subject>RNA-binding domain</subject><subject>SAXS</subject><subject>Scattering, Small Angle</subject><subject>Structural Biology</subject><subject>structure</subject><issn>2059-7983</issn><issn>2059-7983</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU-P0zAQxSMEYlfLfgAuKEc4ZLHjOI4vSKW7tEhtEXTFn5M1dSatIU2K7exS7nxvHKVbLXDgZOvNe7_RzETRU0ouKCXi5TIlXApZMMpJmrG0eBCd9lLSaw_v_U-ic-e-EkJozgRl2ePoJM0LmeW5OI1-Lb3ttO8s1LHegAXt0Zqf4E3bxG0V-w3GiyRoW9MEyw6sv5PnVx-Wybj9GDedrrHVsHOmjFf7-HNiYR-Xpqp6XA-CpozdFuo6gWZd48HhNPi-W7N-Ej2qoHZ4fnjPous3V9fjaTJ7N3k7Hs0SzVPKkwpLsULJc40FTQsmWUqxLHJAzjKQgIKUTOSF0GFDnArKRZWVmAHPoVxV7Cx6NWB33WqLpcbGh7nVzpot2L1qwag_K43ZqHV7owJJcpkFwIsBsPkrNh3NVK8RmjFJCnJDg_f5oZltv3fovNoap7GuocG2c4qKXOSpoBkJVjpYtW2ds1gd2ZSo_tjqn2OHzLP7sxwTd6cNBjkYbk2N-_8T1ejLZTpf8LC5kE2GrHEefxyzYL-pQBZcfVpM1Gs6mc7I_L2i7DfgJ8Un</recordid><startdate>201602</startdate><enddate>201602</enddate><creator>Papageorgiou, Nicolas</creator><creator>Lichière, Julie</creator><creator>Baklouti, Amal</creator><creator>Ferron, François</creator><creator>Sévajol, Marion</creator><creator>Canard, Bruno</creator><creator>Coutard, Bruno</creator><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8351-4992</orcidid><orcidid>https://orcid.org/0000-0002-2859-7123</orcidid><orcidid>https://orcid.org/0000-0003-4924-1991</orcidid></search><sort><creationdate>201602</creationdate><title>Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering</title><author>Papageorgiou, Nicolas ; Lichière, Julie ; Baklouti, Amal ; Ferron, François ; Sévajol, Marion ; Canard, Bruno ; Coutard, Bruno</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5215-fed7be956ce812839321ed86ae534a9ae70d37687c110517157f4de4a56adbf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Biochemistry, Molecular Biology</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Life Sciences</topic><topic>MERS-CoV</topic><topic>Middle East Respiratory Syndrome Coronavirus - chemistry</topic><topic>Models, Molecular</topic><topic>nucleocapsid</topic><topic>Nucleocapsid Proteins - chemistry</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Tertiary</topic><topic>Quantitative Methods</topic><topic>Research Papers</topic><topic>RNA-binding domain</topic><topic>SAXS</topic><topic>Scattering, Small Angle</topic><topic>Structural Biology</topic><topic>structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Papageorgiou, Nicolas</creatorcontrib><creatorcontrib>Lichière, Julie</creatorcontrib><creatorcontrib>Baklouti, Amal</creatorcontrib><creatorcontrib>Ferron, François</creatorcontrib><creatorcontrib>Sévajol, Marion</creatorcontrib><creatorcontrib>Canard, Bruno</creatorcontrib><creatorcontrib>Coutard, Bruno</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section D, Structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Papageorgiou, Nicolas</au><au>Lichière, Julie</au><au>Baklouti, Amal</au><au>Ferron, François</au><au>Sévajol, Marion</au><au>Canard, Bruno</au><au>Coutard, Bruno</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering</atitle><jtitle>Acta crystallographica. Section D, Structural biology</jtitle><addtitle>Acta Cryst. D</addtitle><date>2016-02</date><risdate>2016</risdate><volume>72</volume><issue>2</issue><spage>192</spage><epage>202</epage><pages>192-202</pages><issn>2059-7983</issn><eissn>2059-7983</eissn><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.
The structural characterization of the N‐terminal part of the nucleocapsid from Middle East respiratory syndrome coronavirus (MERS‐CoV), a recently emerging virus, is reported. The structure of the N‐terminal region, which includes a disordered tail followed by a globular domain, was obtained by combining X‐ray diffraction and SAXS.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>26894667</pmid><doi>10.1107/S2059798315024328</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-8351-4992</orcidid><orcidid>https://orcid.org/0000-0002-2859-7123</orcidid><orcidid>https://orcid.org/0000-0003-4924-1991</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry, Molecular Biology Crystallization Crystallography, X-Ray Life Sciences MERS-CoV Middle East Respiratory Syndrome Coronavirus - chemistry Models, Molecular nucleocapsid Nucleocapsid Proteins - chemistry Protein Multimerization Protein Structure, Tertiary Quantitative Methods Research Papers RNA-binding domain SAXS Scattering, Small Angle Structural Biology structure |
| title | Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering |
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