title: Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.
abstract: 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), Taï 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 [Dziubańska 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.
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Laura E
authors.initials: LE
authors.lastname: Baker
authors.affiliation: Department of Chemistry, University of Virginia, Charlottesville, VA 22904-4319, USA.
authors.forename: Jeffrey F
authors.initials: JF
authors.lastname: Ellena
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Katarzyna B
authors.initials: KB
authors.lastname: Handing
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Urszula
authors.initials: U
authors.lastname: Derewenda
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Darkhan
authors.initials: D
authors.lastname: Utepbergenov
authors.affiliation: Department of Microbiology, Immunology and Cancer Biology, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Daniel A
authors.initials: DA
authors.lastname: Engel
authors.affiliation: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908-0736, USA.
authors.forename: Zygmunt S
authors.initials: ZS
authors.lastname: Derewenda
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D029043:Ebolavirus / Q000737:chemistry*; D019142:Hemorrhagic Fever, Ebola / Q000821:virology; D008379:Marburg Virus Disease / Q000821:virology; D029024:Marburgvirus / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009698:Nucleoproteins / Q000737:chemistry*; D011487:Protein Conformation; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D009698:Nucleoproteins; D014764:Viral Proteins
keywords: Ebolavirus; Filoviridae; Marburgvirus; nucleoprotein; viral proteins