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Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering

Identifieur interne : 000A00 ( Pmc/Checkpoint ); précédent : 000999; suivant : 000A01

Structural 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 Coutard

Source :

RBID : PMC:7159594

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.


Url:
DOI: 10.1107/S2059798315024328
PubMed: 26894667
PubMed Central: 7159594


Affiliations:


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PMC:7159594

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<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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Aix-Marseille Université, AFMB UMR 7257, 13288Marseille, France</aff>
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Nicolas Papageorgiou, e-mail:
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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>
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<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.
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