
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.
Keywords: nucleoproteins; Middle East respiratory syndrome coronavirus; MERS-CoV; Coronaviridae; X-ray diffraction; SAXS.
Supporting information
![]() | Portable Document Format (PDF) file https://doi.org/10.1107/S2059798318014948/mn5116sup1.pdf |
PDB reference: C-terminal domain of MERS-CoV nucleocapsid, 6g13