4QAZ
The crystal structure of the C-terminal domain of Ebola (Zaire) nucleoprotein
4QAZ の概要
| エントリーDOI | 10.2210/pdb4qaz/pdb |
| 関連するPDBエントリー | 4QB0 |
| 分子名称 | Nucleoprotein (2 entities in total) |
| 機能のキーワード | new family, ebola virus vp40, viral protein |
| 由来する生物種 | Ebola virus (ZEBOV) |
| 細胞内の位置 | Virion: P18272 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12339.70 |
| 構造登録者 | Derewenda, U.,Dziubanska, P.J.,Derewenda, Z.S. (登録日: 2014-05-06, 公開日: 2014-09-10, 最終更新日: 2024-02-28) |
| 主引用文献 | Dziubanska, P.J.,Derewenda, U.,Ellena, J.F.,Engel, D.A.,Derewenda, Z.S. The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein. Acta Crystallogr.,Sect.D, 70:2420-2429, 2014 Cited by PubMed Abstract: 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 Å resolution is described. The structure reveals a novel tertiary fold that is distantly reminiscent of the β-grasp architecture. PubMed: 25195755DOI: 10.1107/S1399004714014710 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.98 Å) |
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