Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein - Archive ouverte HAL Access content directly
Journal Articles Acta crystallographica Section D : Structural biology [1993-...] Year : 2019

Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) is a human pathogen responsible for a severe respiratory illness that emerged in 2012. Structural information about the proteins that constitute the viral particle is scarce. In order to contribute to a better understanding of the nucleoprotein (N) in charge of RNA genome encapsidation, the structure of the C-terminal domain of N from MERS-CoV obtained using single-crystal X-ray diffraction is reported here at 1.97 Å resolution. The molecule is present as a dimer in the crystal structure and this oligomerization state is confirmed in solution, as measured by additional methods including small-angle X-ray scattering measurements. Comparisons with the structures of the C-terminal domains of N from other coronaviruses reveals a high degree of structural conservation despite low sequence conservation, and differences in electrostatic potential at the surface of the protein.
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inserm-02416977 , version 1 (17-12-2019)

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Thi Hong Van Nguyen, Julie Lichiere, Bruno Canard, Nicolas Papageorgiou, Sarah Attoumani, et al.. Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein. Acta crystallographica Section D : Structural biology [1993-..], 2019, 75 (1), pp.8-15. ⟨10.1107/S2059798318014948⟩. ⟨inserm-02416977⟩
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