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 ==The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein==
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 == Publication Abstract from PubMed ==
-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 A resolution is described. The structure reveals a novel tertiary fold that is distantly reminiscent of the beta-grasp architecture.
+The Filoviridae family of negative-sense, single-stranded RNA (ssRNA) viruses is comprised of two species of Marburgvirus (MARV and RAVV) and five species of Ebolavirus, i.e. Zaire (EBOV), Reston (RESTV), Sudan (SUDV), Tai Forest (TAFV) and Bundibugyo (BDBV). In each of these viruses the 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. It is tightly associated with the viral RNA in the nucleocapsid, and during the lifecycle of the virus is essential for transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. The structure of the unique C-terminal globular domain of the NP from EBOV has recently been determined and shown to be structurally unrelated to any other known protein [Dziubanska et al. (2014), Acta Cryst. D70, 2420-2429]. In this paper, a study of the C-terminal domains from the NP from the remaining four species of Ebolavirus, as well as from the MARV strain of Marburgvirus, is reported. As expected, the crystal structures of the BDBV and TAFV proteins show high structural similarity to that from EBOV, while the MARV protein behaves like a molten globule with a core residual structure that is significantly different from that of the EBOV protein.
-The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein.,Dziubanska PJ, Derewenda U, Ellena JF, Engel DA, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2420-9. doi:, 10.1107/S1399004714014710. Epub 2014 Aug 29. PMID:25195755<ref>PMID:25195755</ref>
+Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.,Baker LE, Ellena JF, Handing KB, Derewenda U, Utepbergenov D, Engel DA, Derewenda ZS Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):49-58. doi:, 10.1107/S2059798315021439. Epub 2016 Jan 1. PMID:26894534<ref>PMID:26894534</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>