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

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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Supporting information

Supporting information for this article can be found http://scripts.iucr.org/cgi-bin/paper?mn5105