Structural characterization of the N‐terminal part of the MERS‐CoV nucleocapsid by X‐ray diffraction and small‐angle X‐ray scattering
Identifieur interne : 000C15 ( Main/Exploration ); précédent : 000C14; suivant : 000C16Structural 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 [ 2059-7983 ] ; 2016-02-01.
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.
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DOI: 10.1107/S2059798315024328
Affiliations:
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<front><div type="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.</div>
<div type="abstract" xml:lang="en">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.</div>
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