5DSD

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

「5CIJ」から置き換えられました

5DSD の概要

• エントリーDOI: 10.2210/pdb5dsd/pdb
• 関連するPDBエントリー: 4QAZ 4QB0
• 分子名称: Nucleoprotein, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: viral protein, filoviridae
• 由来する生物種: Bundibugyo virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12487.37

構造登録者

Baker, L.,Handing, K.B.,Utepbergenov, D.,Derewenda, U.,Derewenda, Z.S. (登録日: 2015-09-17, 公開日: 2015-09-30, 最終更新日: 2023-09-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.31 Å)