Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoprotein.
Acta Crystallogr D Struct Biol
; 75(Pt 1): 8-15, 2019 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-30644840
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 1.97â
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.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Multimerização Proteica
/
Coronavírus da Síndrome Respiratória do Oriente Médio
/
Nucleoproteínas
Limite:
Humans
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article