4UD1

Structure of the N Terminal domain of the MERS CoV nucleocapsid

Summary for 4UD1

• Entry DOI: 10.2210/pdb4ud1/pdb
• Descriptor: N PROTEIN, AMMONIUM ION, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: viral protein, rna binding domain
• Biological source: MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS (MERS-COV)
• Total number of polymer chains: 5
• Total formula weight: 89530.25

Authors

Papageorgiou, N.,Lichiere, J.,Ferron, F.,Canard, B.,Coutard, B. (deposition date: 2014-12-05, release date: 2015-12-02, Last modification date: 2023-12-20)

Primary citation

Papageorgiou, N.,Lichiere, J.,Baklouti, A.,Ferron, F.,Canard, B.,Coutard, B.
Structural Characterization of the N-Terminal Part of the Mers-Cov Nucleocapsid by X-Ray Diffraction and Small-Angle X-Ray Scattering
Acta Crystallogr.,Sect.D, 72:192-, 2016

PubMed Abstract: The N protein of coronaviruses is a multifunctional protein that is organized into several domains. The N-terminal part is composed of an intrinsically disordered region (IDR) followed by a structured domain called the N-terminal domain (NTD). In this study, the structure determination of the N-terminal region of the MERS-CoV N protein via X-ray diffraction measurements is reported at a resolution of 2.4 Å. Since the first 30 amino acids were not resolved by X-ray diffraction, the structural study was completed by a SAXS experiment to propose a structural model including the IDR. This model presents the N-terminal region of the MERS-CoV as a monomer that displays structural features in common with other coronavirus NTDs.

PubMed: 26894667
DOI: 10.1107/S2059798315024328

Experimental method

X-RAY DIFFRACTION (2.48 Å)