4QB0

The crystal structure of the C-terminal domain of Ebola (Zaire) nucleoprotein

Summary for 4QB0

• Entry DOI: 10.2210/pdb4qb0/pdb
• Related: 4QAZ
• Descriptor: Nucleoprotein (2 entities in total)
• Functional Keywords: new family, ebola virus vp40, viral protein
• Biological source: Ebola virus (ZEBOV)
• Cellular location: Virion: P18272
• Total number of polymer chains: 1
• Total formula weight: 12339.70

Authors

Derewenda, U.,Dziubanska, P.J.,Derewenda, Z.S. (deposition date: 2014-05-06, release date: 2014-09-10, Last modification date: 2024-02-28)

Primary citation

Dziubanska, P.J.,Derewenda, U.,Ellena, J.F.,Engel, D.A.,Derewenda, Z.S.
The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein.
Acta Crystallogr.,Sect.D, 70:2420-2429, 2014

PubMed Abstract: Ebolavirus (EBOV) causes severe hemorrhagic fever with a mortality rate of up to 90%. EBOV is a member of the order Mononegavirales and, like other viruses in this taxonomic group, contains a negative-sense single-stranded (ss) RNA. The EBOV ssRNA encodes seven distinct proteins. One of them, the nucleoprotein (NP), is the most abundant viral protein in the infected cell and within the viral nucleocapsid. Like other EBOV proteins, NP is multifunctional. It is tightly associated with the viral genome and is essential for viral transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. NP is unusual among the Mononegavirales in that it contains two distinct regions, or putative domains, the C-terminal of which shows no homology to any known proteins and is purported to be a hub for protein-protein interactions within the nucleocapsid. The atomic structure of NP remains unknown. Here, the boundaries of the N- and C-terminal domains of NP from Zaire EBOV are defined, it is shown that they can be expressed as highly stable recombinant proteins in Escherichia coli, and the atomic structure of the C-terminal domain (residues 641-739) derived from analysis of two distinct crystal forms at 1.98 and 1.75 Å resolution is described. The structure reveals a novel tertiary fold that is distantly reminiscent of the β-grasp architecture.

PubMed: 25195755
DOI: 10.1107/S1399004714014710

Experimental method

X-RAY DIFFRACTION (1.75 Å)