6G13

C-terminal domain of MERS-CoV nucleocapsid

Summary for 6G13

• Entry DOI: 10.2210/pdb6g13/pdb
• Descriptor: Nucleoprotein, trimethylamine oxide, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: nucleocapsid, rna binding protein, mers, coronavirus, ctd, viral protein
• Biological source: Middle East respiratory syndrome-related coronavirus
• Total number of polymer chains: 4
• Total formula weight: 57418.29

Authors

Nguyen, T.H.V.,Ferron, F.P.,Lichiere, J.,Canard, B.,Papageorgiou, N.,Coutard, B. (deposition date: 2018-03-20, release date: 2019-02-27, Last modification date: 2024-01-17)

Primary citation

Nguyen, T.H.V.,Lichiere, J.,Canard, B.,Papageorgiou, N.,Attoumani, S.,Ferron, F.,Coutard, B.
Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.
Acta Crystallogr D Struct Biol, 75:8-15, 2019

PubMed 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.

PubMed: 30644840
DOI: 10.1107/S2059798318014948

Experimental method

X-RAY DIFFRACTION (1.97 Å)