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

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


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

MeSH terms

  • Humans
  • Middle East Respiratory Syndrome Coronavirus / chemistry*
  • Molecular Structure
  • Nucleoproteins / chemistry*
  • Protein Multimerization*
  • Scattering, Small Angle
  • Static Electricity
  • Viral Proteins / chemistry
  • X-Ray Diffraction


  • Nucleoproteins
  • Viral Proteins