The structure of the C‐terminal domain of the Zaire ebolavirus nucleoprotein. (1st September 2014)

• Record Type: Journal Article
• Authors: Dziubańska, Paulina J.; Derewenda, Urszula; Ellena, Jeffrey F.; Engel, Daniel A.; Derewenda, Zygmunt S.
• Is Part Of: Acta crystallographica. Volume 70:Part 9(2014:Sep.)
• Page Start: 2420
• Page End: 2429
• Publication Date: 2014-09-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714014710
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Ebolavirus</italic> (EBOV) causes severe hemorrhagic fever with a mortality rate of up to 90%. EBOV is a member of the order <italic>Mononegavirales</italic> 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 <italic>Mononegavirales</italic> 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 <italic>Escherichia coli</italic>, 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.</p> </abstract>