Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Identifieur interne : 000977 ( Pmc/Curation ); précédent : 000976; suivant : 000978Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Auteurs : Nicolas Papageorgiou ; Julie Lichière ; Amal Baklouti ; François Ferron ; Marion Sévajol ; Bruno Canard ; Bruno CoutardSource :
- Acta Crystallographica. Section D, Structural Biology [ 2059-7983 ] ; 2016.
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
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DOI: 10.1107/S2059798315024328
PubMed: 26894667
PubMed Central: 7159594
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<front><div type="abstract" xml:lang="en"><p>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 <italic>via</italic>
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.</p>
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<title-group><article-title>Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering</article-title>
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<aff id="AYD2MN5105-aff-a1"><label><sup>1</sup>
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CNRS, AFMB UMR 7257, 13288Marseille, France</aff>
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Aix-Marseille Université, AFMB UMR 7257, 13288Marseille, France</aff>
<author-notes><corresp id="correspondenceTo"><label>*</label>
Nicolas Papageorgiou, e-mail: <email>nicolas.papageorgiou@afmb.univ-mrs.fr</email>
; Bruno Coutard, e-mail: <email>bruno.coutard@afmb.univ-mrs.fr</email>
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<month>10</month>
<year>2015</year>
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<permissions><copyright-statement content-type="article-copyright">© International Union of Crystallography, 2016</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>
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<abstract><p>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 <italic>via</italic>
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.</p>
</abstract>
<abstract abstract-type="graphical"><p>The structural characterization of the N‐terminal part of the nucleocapsid from <italic>Middle East respiratory syndrome coronavirus</italic>
(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.<boxed-text position="anchor" content-type="graphic" orientation="portrait"><graphic xlink:href="AYD2-72-192-g001.jpg" position="anchor" id="nlm-graphic-1" orientation="portrait"></graphic>
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