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Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):8-15. doi: 10.1107/S2059798318014948. Epub 2019 Jan 4.

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

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Aix-Marseille Université, AFMB UMR 7257, 13288 Marseilles, France.


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.


Coronaviridae; MERS-CoV; Middle East respiratory syndrome coronavirus; SAXS; X-ray diffraction; nucleoproteins

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