5DSD

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

Replaces:  5CIJ

Summary for 5DSD

• Entry DOI: 10.2210/pdb5dsd/pdb
• Related: 4QAZ 4QB0
• Descriptor: Nucleoprotein, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: viral protein, filoviridae
• Biological source: Bundibugyo virus
• Total number of polymer chains: 1
• Total formula weight: 12487.37

Authors

Baker, L.,Handing, K.B.,Utepbergenov, D.,Derewenda, U.,Derewenda, Z.S. (deposition date: 2015-09-17, release date: 2015-09-30, Last modification date: 2023-09-27)

Primary citation

Baker, L.E.,Ellena, J.F.,Handing, K.B.,Derewenda, U.,Utepbergenov, D.,Engel, D.A.,Derewenda, Z.S.
Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.
Acta Crystallogr D Struct Biol, 72:49-58, 2016

PubMed 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.

PubMed: 26894534
DOI: 10.1107/S2059798315021439

Experimental method

X-RAY DIFFRACTION (2.31 Å)