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.
Keywords: nucleoproteins, Middle East respiratory syndrome coronavirus, MERS‐CoV, Coronaviridae, X‐ray diffraction, SAXS
The X‐ray structure and SAXS analysis of the C‐terminal domain of the nucleocapsid from Middle East respiratory syndrome coronavirus, an emerging virus, are reported.
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Supporting information for this article can be found http://scripts.iucr.org/cgi-bin/paper?mn5116
Contributor Information
François Ferron, Email: francois.ferron@afmb.univ-mrs.fr.
Bruno Coutard, Email: bruno.coutard@afmb.univ-mrs.fr.
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Supplementary Materials
Supporting information for this article can be found http://scripts.iucr.org/cgi-bin/paper?mn5116